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	<id>https://proteopedia.org/api.php?action=feedcontributions&amp;feedformat=atom&amp;user=Jing+Liu</id>
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	<updated>2026-09-16T13:53:59Z</updated>
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	<entry>
		<id>https://proteopedia.org/index.php?title=Molecular_Playground/DNA_replication_initiator_DnaA&amp;diff=2065456</id>
		<title>Molecular Playground/DNA replication initiator DnaA</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=Molecular_Playground/DNA_replication_initiator_DnaA&amp;diff=2065456"/>
		<updated>2014-11-19T15:08:05Z</updated>

		<summary type="html">&lt;p&gt;Jing Liu: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;One of the [[CBI Molecules]] being studied in the  [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&amp;lt;Structure load=&#039;1L8Q&#039; size=&#039;400&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;DnaA residues 76-399 complex with ADP and Mg+2 ion, [[1l8q]]&#039; scene=&#039;User:Jing_Liu/Sandbox_1/1/4&#039; /&amp;gt;&lt;br /&gt;
This is a &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/4&#039;&amp;gt;DnaA monomer strucure(residues 76-399)&amp;lt;/scene&amp;gt;, which contains an &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/5&#039;&amp;gt;ADP&amp;lt;/scene&amp;gt; in it.&lt;br /&gt;
&lt;br /&gt;
=== DnaA function in Prokaryotes===&lt;br /&gt;
&#039;&#039;&#039;DnaA&#039;&#039;&#039; is an AAA+ protein in prokaryotes for DNA replication initiation. To ensure correct timing of DNA replication, intracellular DnaA is under multi-level control, including changing expression/degradation level, regulator control and functional activation/inactivation by nucleotide-depedent conformational change. DnaA is a conserved protein in prokaryotes. In &#039;&#039;E. coli&#039;&#039;, There are four regions in this protein[http://www.ncbi.nlm.nih.gov/pubmed/10572294]:&lt;br /&gt;
&lt;br /&gt;
I: residues 1-85. DnaB loading domain;&lt;br /&gt;
II: residues 86-133. linker region;&lt;br /&gt;
III: residues 134-372. ATPase domain;&lt;br /&gt;
IV: residues 373-467. DNA binding domain;&lt;br /&gt;
&lt;br /&gt;
DnaA function is regulated by different nucleotide binding state. In ATP bound state, DnaA can recognize more binding elements on the chromosome(called DnaA box), and initiate replication by unwinding specific region in the DNA and recruit DnaB helicase. However, after the ATP hydrolysis, DnaA-ADP becomes an inactive protein. This activity change was shown to be associated with its oligomeric assembly state.  &lt;br /&gt;
&lt;br /&gt;
=== DnaA Monomer Structure ===&lt;br /&gt;
The &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/4&#039;&amp;gt;structure of DnaA&amp;lt;/scene&amp;gt; in &#039;&#039;Aquifex aeolicus&#039;&#039; was solved in 2002[http://www.ncbi.nlm.nih.gov/pubmed/12234917?dopt=Abstract], and it contains the linker region, AAA+ domain and DNA binding domain(DBD). The interaction with DNA is through the recognization of a conserved 9 bp DNA recognition sequence (TTA/TTNCACC), and this was shown by the crystal structure of the &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/2/1&#039;&amp;gt;complex&amp;lt;/scene&amp;gt; in &#039;&#039;Mycobacterium tuberculosis&#039;&#039;[http://www.ncbi.nlm.nih.gov/pubmed/21620858?dopt=Abstract]. &lt;br /&gt;
&lt;br /&gt;
=== Distinct Assembly State of DnaA ===&lt;br /&gt;
&amp;lt;Structure load=&#039;1L8Q&#039; size=&#039;300&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;2HCB tetramer&#039; scene=&#039;User:Jing_Liu/Sandbox_1/3/3&#039; /&amp;gt;&lt;br /&gt;
The crystal structure of AMP-PCP-bound DnaA reveals a &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/3/3&#039;&amp;gt;right-handed superhelix&amp;lt;/scene&amp;gt; structure[http://www.ncbi.nlm.nih.gov/pubmed/16829961?dopt=Abstract]. Each monomer contact with another two monomers to form a filamentous structure. The engagement of ATP involved the arginine figure at position 230.&lt;br /&gt;
&lt;br /&gt;
=== Reference ===&lt;br /&gt;
1. Messer, W., et al., Functional domains of DnaA proteins. Biochimie, 1999. 81(8-9): p. 819-25.&lt;br /&gt;
&lt;br /&gt;
2. Erzberger, J.P., et al., The structure of bacterial DnaA: implications for general mechanisms underlying DNA replication initiation. EMBO J. 2002 Sep 16;21(18):4763-73.&lt;br /&gt;
&lt;br /&gt;
3. Tsodikov OV and Biswas T. Structural and thermodynamic signatures of DNA recognition by Mycobacterium tuberculosis DnaA. J Mol Biol. 2011 Jul 15;410(3):461-76. Epub 2011 May 18.&lt;br /&gt;
&lt;br /&gt;
4. Erzberger, J.P., et al., Structural basis for ATP-dependent DnaA assembly and replication-origin remodeling. Nat Struct Mol Biol. 2006 Aug;13(8):676-83. Epub 2006 Jul 9.&lt;/div&gt;</summary>
		<author><name>Jing Liu</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=Molecular_Playground/DNA_replication_initiator_DnaA&amp;diff=2065455</id>
		<title>Molecular Playground/DNA replication initiator DnaA</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=Molecular_Playground/DNA_replication_initiator_DnaA&amp;diff=2065455"/>
		<updated>2014-11-19T15:06:56Z</updated>

		<summary type="html">&lt;p&gt;Jing Liu: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;One of the [[CBI Molecules]] being studied in the  [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&amp;lt;Structure load=&#039;1L8Q&#039; size=&#039;400&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;DnaA residues 76-399 complex with ADP and Mg+2 ion, [[1l8q]]&#039; scene=&#039;User:Jing_Liu/Sandbox_1/1/4&#039; /&amp;gt;&lt;br /&gt;
This is a &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/4&#039;&amp;gt;DnaA monomer strucure(residues 76-399)&amp;lt;/scene&amp;gt;, which contains an &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/5&#039;&amp;gt;ADP&amp;lt;/scene&amp;gt; in it.&lt;br /&gt;
&lt;br /&gt;
=== DnaA function in Prokaryotes===&lt;br /&gt;
&#039;&#039;&#039;DnaA&#039;&#039;&#039; is an AAA+ protein in prokaryotes for DNA replication initiation. To ensure correct timing of DNA replication, intracellular DnaA is under multi-level control, including changing expression/degradation level, regulator control and functional activation/inactivation by nucleotide-depedent conformational change. DnaA is a conserved protein in prokaryotes. In &#039;&#039;E. coli&#039;&#039;, There are four regions in this protein[http://www.ncbi.nlm.nih.gov/pubmed/10572294]:&lt;br /&gt;
&lt;br /&gt;
I: residues 1-85. DnaB loading domain;&lt;br /&gt;
II: residues 86-133. linker region;&lt;br /&gt;
III: residues 134-372. ATPase domain;&lt;br /&gt;
IV: residues 373-467. DNA binding domain;&lt;br /&gt;
&lt;br /&gt;
DnaA function is regulated by different nucleotide binding state. In ATP bound state, DnaA can recognize more binding elements on the chromosome(called DnaA box), and initiate replication by unwinding specific region in the DNA and recruit DnaB helicase. However, after the ATP hydrolysis, DnaA-ADP becomes an inactive protein. This activity change was shown to be associated with its oligomeric assembly state.  &lt;br /&gt;
&amp;lt;Structure load=&#039;4u0g&#039; size=&#039;400&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;test&#039; scene=&#039;49/493690/Test/1&#039; /&amp;gt;&lt;br /&gt;
This is a &amp;lt;scene name=&#039;49/493690/Test/1&#039;&amp;gt;test(residues 76-399)&amp;lt;/scene&amp;gt;, which contains an &amp;lt;scene name=&#039;49/493690/Test/1&#039;&amp;gt;ADP&amp;lt;/scene&amp;gt; in it.&lt;br /&gt;
&amp;lt;scene name=&#039;49/493690/Test/1&#039;&amp;gt;This is a test molecule&amp;lt;/scene&amp;gt;&lt;br /&gt;
=== DnaA Monomer Structure ===&lt;br /&gt;
The &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/4&#039;&amp;gt;structure of DnaA&amp;lt;/scene&amp;gt; in &#039;&#039;Aquifex aeolicus&#039;&#039; was solved in 2002[http://www.ncbi.nlm.nih.gov/pubmed/12234917?dopt=Abstract], and it contains the linker region, AAA+ domain and DNA binding domain(DBD). The interaction with DNA is through the recognization of a conserved 9 bp DNA recognition sequence (TTA/TTNCACC), and this was shown by the crystal structure of the &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/2/1&#039;&amp;gt;complex&amp;lt;/scene&amp;gt; in &#039;&#039;Mycobacterium tuberculosis&#039;&#039;[http://www.ncbi.nlm.nih.gov/pubmed/21620858?dopt=Abstract]. &lt;br /&gt;
&lt;br /&gt;
=== Distinct Assembly State of DnaA ===&lt;br /&gt;
&amp;lt;Structure load=&#039;1L8Q&#039; size=&#039;300&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;2HCB tetramer&#039; scene=&#039;User:Jing_Liu/Sandbox_1/3/3&#039; /&amp;gt;&lt;br /&gt;
The crystal structure of AMP-PCP-bound DnaA reveals a &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/3/3&#039;&amp;gt;right-handed superhelix&amp;lt;/scene&amp;gt; structure[http://www.ncbi.nlm.nih.gov/pubmed/16829961?dopt=Abstract]. Each monomer contact with another two monomers to form a filamentous structure. The engagement of ATP involved the arginine figure at position 230.&lt;br /&gt;
&lt;br /&gt;
=== Reference ===&lt;br /&gt;
1. Messer, W., et al., Functional domains of DnaA proteins. Biochimie, 1999. 81(8-9): p. 819-25.&lt;br /&gt;
&lt;br /&gt;
2. Erzberger, J.P., et al., The structure of bacterial DnaA: implications for general mechanisms underlying DNA replication initiation. EMBO J. 2002 Sep 16;21(18):4763-73.&lt;br /&gt;
&lt;br /&gt;
3. Tsodikov OV and Biswas T. Structural and thermodynamic signatures of DNA recognition by Mycobacterium tuberculosis DnaA. J Mol Biol. 2011 Jul 15;410(3):461-76. Epub 2011 May 18.&lt;br /&gt;
&lt;br /&gt;
4. Erzberger, J.P., et al., Structural basis for ATP-dependent DnaA assembly and replication-origin remodeling. Nat Struct Mol Biol. 2006 Aug;13(8):676-83. Epub 2006 Jul 9.&lt;/div&gt;</summary>
		<author><name>Jing Liu</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=Molecular_Playground/DNA_replication_initiator_DnaA&amp;diff=2065453</id>
		<title>Molecular Playground/DNA replication initiator DnaA</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=Molecular_Playground/DNA_replication_initiator_DnaA&amp;diff=2065453"/>
		<updated>2014-11-19T15:04:52Z</updated>

		<summary type="html">&lt;p&gt;Jing Liu: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;One of the [[CBI Molecules]] being studied in the  [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&amp;lt;Structure load=&#039;1L8Q&#039; size=&#039;400&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;DnaA residues 76-399 complex with ADP and Mg+2 ion, [[1l8q]]&#039; scene=&#039;User:Jing_Liu/Sandbox_1/1/4&#039; /&amp;gt;&lt;br /&gt;
This is a &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/4&#039;&amp;gt;DnaA monomer strucure(residues 76-399)&amp;lt;/scene&amp;gt;, which contains an &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/5&#039;&amp;gt;ADP&amp;lt;/scene&amp;gt; in it.&lt;br /&gt;
&lt;br /&gt;
=== DnaA function in Prokaryotes===&lt;br /&gt;
&#039;&#039;&#039;DnaA&#039;&#039;&#039; is an AAA+ protein in prokaryotes for DNA replication initiation. To ensure correct timing of DNA replication, intracellular DnaA is under multi-level control, including changing expression/degradation level, regulator control and functional activation/inactivation by nucleotide-depedent conformational change. DnaA is a conserved protein in prokaryotes. In &#039;&#039;E. coli&#039;&#039;, There are four regions in this protein[http://www.ncbi.nlm.nih.gov/pubmed/10572294]:&lt;br /&gt;
&lt;br /&gt;
I: residues 1-85. DnaB loading domain;&lt;br /&gt;
II: residues 86-133. linker region;&lt;br /&gt;
III: residues 134-372. ATPase domain;&lt;br /&gt;
IV: residues 373-467. DNA binding domain;&lt;br /&gt;
&lt;br /&gt;
DnaA function is regulated by different nucleotide binding state. In ATP bound state, DnaA can recognize more binding elements on the chromosome(called DnaA box), and initiate replication by unwinding specific region in the DNA and recruit DnaB helicase. However, after the ATP hydrolysis, DnaA-ADP becomes an inactive protein. This activity change was shown to be associated with its oligomeric assembly state.  &lt;br /&gt;
&amp;lt;scene name=&#039;49/493690/Test/1&#039;&amp;gt;This is a test molecule&amp;lt;/scene&amp;gt;&lt;br /&gt;
=== DnaA Monomer Structure ===&lt;br /&gt;
The &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/4&#039;&amp;gt;structure of DnaA&amp;lt;/scene&amp;gt; in &#039;&#039;Aquifex aeolicus&#039;&#039; was solved in 2002[http://www.ncbi.nlm.nih.gov/pubmed/12234917?dopt=Abstract], and it contains the linker region, AAA+ domain and DNA binding domain(DBD). The interaction with DNA is through the recognization of a conserved 9 bp DNA recognition sequence (TTA/TTNCACC), and this was shown by the crystal structure of the &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/2/1&#039;&amp;gt;complex&amp;lt;/scene&amp;gt; in &#039;&#039;Mycobacterium tuberculosis&#039;&#039;[http://www.ncbi.nlm.nih.gov/pubmed/21620858?dopt=Abstract]. &lt;br /&gt;
&lt;br /&gt;
=== Distinct Assembly State of DnaA ===&lt;br /&gt;
&amp;lt;Structure load=&#039;1L8Q&#039; size=&#039;300&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;2HCB tetramer&#039; scene=&#039;User:Jing_Liu/Sandbox_1/3/3&#039; /&amp;gt;&lt;br /&gt;
The crystal structure of AMP-PCP-bound DnaA reveals a &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/3/3&#039;&amp;gt;right-handed superhelix&amp;lt;/scene&amp;gt; structure[http://www.ncbi.nlm.nih.gov/pubmed/16829961?dopt=Abstract]. Each monomer contact with another two monomers to form a filamentous structure. The engagement of ATP involved the arginine figure at position 230.&lt;br /&gt;
&lt;br /&gt;
=== Reference ===&lt;br /&gt;
1. Messer, W., et al., Functional domains of DnaA proteins. Biochimie, 1999. 81(8-9): p. 819-25.&lt;br /&gt;
&lt;br /&gt;
2. Erzberger, J.P., et al., The structure of bacterial DnaA: implications for general mechanisms underlying DNA replication initiation. EMBO J. 2002 Sep 16;21(18):4763-73.&lt;br /&gt;
&lt;br /&gt;
3. Tsodikov OV and Biswas T. Structural and thermodynamic signatures of DNA recognition by Mycobacterium tuberculosis DnaA. J Mol Biol. 2011 Jul 15;410(3):461-76. Epub 2011 May 18.&lt;br /&gt;
&lt;br /&gt;
4. Erzberger, J.P., et al., Structural basis for ATP-dependent DnaA assembly and replication-origin remodeling. Nat Struct Mol Biol. 2006 Aug;13(8):676-83. Epub 2006 Jul 9.&lt;/div&gt;</summary>
		<author><name>Jing Liu</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1543513</id>
		<title>User:Jing Liu/Sandbox 1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1543513"/>
		<updated>2012-10-10T16:01:20Z</updated>

		<summary type="html">&lt;p&gt;Jing Liu: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;One of the [[CBI Molecules]] being studied in the  [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
==Your Heading Here (maybe something like &#039;Structure&#039;)==&amp;lt;StructureSection load=&#039;1dq8&#039; size=&#039;300&#039; side=&#039;right&#039; caption=&#039;Structure of HMG-CoA reductase (PDB entry [[1dq8]])&#039; scene=&#039;&#039;&amp;gt;Anything in this section will appear adjacent to the 3D structure and will be scrollable.&lt;br /&gt;
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&amp;lt;/StructureSection&amp;gt;&lt;br /&gt;
&amp;lt;Structure load=&#039;1L8Q&#039; size=&#039;300&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;1L8Q 76-399&#039; scene=&#039;User:Jing_Liu/Sandbox_1/1/4&#039; /&amp;gt;&lt;br /&gt;
This is a &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/4&#039;&amp;gt;DnaA monomer strucure(residues 76-399)&amp;lt;/scene&amp;gt;, which contains an &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/5&#039;&amp;gt;ADP&amp;lt;/scene&amp;gt; in it.&lt;br /&gt;
&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
----&lt;br /&gt;
=== DnaA function in Prokaryotes===&lt;br /&gt;
DnaA is an AAA+ protein in prokaryotes for DNA replication initiation. To ensure correct timing of DNA replication, intracellular DnaA is under multi-level control, including changing expression/degradation level, regulator control and functional activation/inactivation by nucleotide-depedent conformational change. DnaA is a conserved protein in prokaryotes. In &#039;&#039;E. coli&#039;&#039;, There are four regions in this protein[http://www.ncbi.nlm.nih.gov/pubmed/10572294]:&lt;br /&gt;
&lt;br /&gt;
I: residues 1-85. DnaB loading domain;&lt;br /&gt;
&lt;br /&gt;
II: residues 86-133. linker region;&lt;br /&gt;
&lt;br /&gt;
III: residues 134-372. ATPase domain;&lt;br /&gt;
&lt;br /&gt;
IV: residues 373-467. DNA binding domain;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
DnaA function is regulated by different nucleotide binding state. In ATP bound state, DnaA can recognize more binding elements on the chromosome(called DnaA box), and initiate replication by unwinding specific region in the DNA and recruit DnaB helicase. However, after the ATP hydrolysis, DnaA-ADP becomes an inactive protein. This activity change was shown to be associated with its oligomeric assembly state.  &lt;br /&gt;
&lt;br /&gt;
=== DnaA Monomer Structure ===&lt;br /&gt;
The &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/4&#039;&amp;gt;structure of DnaA&amp;lt;/scene&amp;gt; in &#039;&#039;Aquifex aeolicus&#039;&#039; was solved in 2002[http://www.ncbi.nlm.nih.gov/pubmed/12234917?dopt=Abstract], and it contains the linker region, AAA+ domain and DNA binding domain(DBD). The interaction with DNA is through the recognization of a conserved 9 bp DNA recognition sequence (TTA/TTNCACC), and this was shown by the crystal structure of the &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/2/1&#039;&amp;gt;complex&amp;lt;/scene&amp;gt; in &#039;&#039;Mycobacterium tuberculosis&#039;&#039;[http://www.ncbi.nlm.nih.gov/pubmed/21620858?dopt=Abstract]. &lt;br /&gt;
&lt;br /&gt;
=== Distinct Assembly State of DnaA ===&lt;br /&gt;
&amp;lt;Structure load=&#039;1L8Q&#039; size=&#039;300&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;2HCB tetramer&#039; scene=&#039;User:Jing_Liu/Sandbox_1/3/3&#039; /&amp;gt;&lt;br /&gt;
The crystal structure of AMP-PCP-bound DnaA reveals a &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/3/3&#039;&amp;gt;right-handed superhelix&amp;lt;/scene&amp;gt; structure[http://www.ncbi.nlm.nih.gov/pubmed/16829961?dopt=Abstract]. Each monomer contact with another two monomers to form a filamentous structure. The engagement of ATP involved the arginine figure at position 230.&lt;br /&gt;
&lt;br /&gt;
=== Reference ===&lt;br /&gt;
1. Messer, W., et al., Functional domains of DnaA proteins. Biochimie, 1999. 81(8-9): p. 819-25.&lt;br /&gt;
&lt;br /&gt;
2. Erzberger, J.P., et al., The structure of bacterial DnaA: implications for general mechanisms underlying DNA replication initiation. EMBO J. 2002 Sep 16;21(18):4763-73.&lt;br /&gt;
&lt;br /&gt;
3. Tsodikov OV and Biswas T. Structural and thermodynamic signatures of DNA recognition by Mycobacterium tuberculosis DnaA. J Mol Biol. 2011 Jul 15;410(3):461-76. Epub 2011 May 18.&lt;br /&gt;
&lt;br /&gt;
4. Erzberger, J.P., et al., Structural basis for ATP-dependent DnaA assembly and replication-origin remodeling. Nat Struct Mol Biol. 2006 Aug;13(8):676-83. Epub 2006 Jul 9.&lt;/div&gt;</summary>
		<author><name>Jing Liu</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1543508</id>
		<title>User:Jing Liu/Sandbox 1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1543508"/>
		<updated>2012-10-10T15:39:26Z</updated>

		<summary type="html">&lt;p&gt;Jing Liu: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;One of the [[CBI Molecules]] being studied in the  [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].&lt;br /&gt;
&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
----&lt;br /&gt;
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==Your Heading Here (maybe something like &#039;Structure&#039;)==&amp;lt;StructureSection load=&#039;1dq8&#039; size=&#039;300&#039; side=&#039;right&#039; caption=&#039;Structure of HMG-CoA reductase (PDB entry [[1dq8]])&#039; scene=&#039;&#039;&amp;gt;Anything in this section will appear adjacent to the 3D structure and will be scrollable.&lt;br /&gt;
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&amp;lt;Structure load=&#039;1L8Q&#039; size=&#039;300&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;1L8Q 76-399&#039; scene=&#039;User:Jing_Liu/Sandbox_1/1/4&#039; /&amp;gt;&lt;br /&gt;
This is a &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/4&#039;&amp;gt;DnaA monomer strucure(residues 76-399)&amp;lt;/scene&amp;gt;, which contains an &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/5&#039;&amp;gt;ADP&amp;lt;/scene&amp;gt; in it.&lt;br /&gt;
&lt;br /&gt;
=== DnaA function in Prokaryotes===&lt;br /&gt;
DnaA is an AAA+ protein in prokaryotes for DNA replication initiation. To ensure correct timing of DNA replication, intracellular DnaA is under multi-level control, including changing expression/degradation level, regulator control and functional activation/inactivation by nucleotide-depedent conformational change. DnaA is a conserved protein in prokaryotes. In &#039;&#039;E. coli&#039;&#039;, There are four regions in this protein[http://www.ncbi.nlm.nih.gov/pubmed/10572294]:&lt;br /&gt;
&lt;br /&gt;
I: residues 1-85. DnaB loading domain;&lt;br /&gt;
&lt;br /&gt;
II: residues 86-133. linker region;&lt;br /&gt;
&lt;br /&gt;
III: residues 134-372. ATPase domain;&lt;br /&gt;
&lt;br /&gt;
IV: residues 373-467. DNA binding domain;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
DnaA function is regulated by different nucleotide binding state. In ATP bound state, DnaA can recognize more binding elements on the chromosome(called DnaA box), and initiate replication by unwinding specific region in the DNA and recruit DnaB helicase. However, after the ATP hydrolysis, DnaA-ADP becomes an inactive protein. This activity change was shown to be associated with its oligomeric assembly state.  &lt;br /&gt;
&lt;br /&gt;
=== DnaA Monomer Structure ===&lt;br /&gt;
The &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/4&#039;&amp;gt;structure of DnaA&amp;lt;/scene&amp;gt; in &#039;&#039;Aquifex aeolicus&#039;&#039; was solved in 2002[http://www.ncbi.nlm.nih.gov/pubmed/12234917?dopt=Abstract], and it contains the linker region, AAA+ domain and DNA binding domain(DBD). The interaction with DNA is through the recognization of a conserved 9 bp DNA recognition sequence (TTA/TTNCACC), and this was shown by the crystal structure of the &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/2/1&#039;&amp;gt;complex&amp;lt;/scene&amp;gt; in &#039;&#039;Mycobacterium tuberculosis&#039;&#039;[http://www.ncbi.nlm.nih.gov/pubmed/21620858?dopt=Abstract]. &lt;br /&gt;
&lt;br /&gt;
=== Distinct Assembly State of DnaA ===&lt;br /&gt;
&amp;lt;Structure load=&#039;1L8Q&#039; size=&#039;300&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;2HCB tetramer&#039; scene=&#039;User:Jing_Liu/Sandbox_1/3/3&#039; /&amp;gt;&lt;br /&gt;
The crystal structure of AMP-PCP-bound DnaA reveals a &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/3/3&#039;&amp;gt;right-handed superhelix&amp;lt;/scene&amp;gt; structure[http://www.ncbi.nlm.nih.gov/pubmed/16829961?dopt=Abstract]. Each monomer contact with another two monomers to form a filamentous structure. The engagement of ATP involved the arginine figure at position 230.&lt;br /&gt;
&lt;br /&gt;
=== Reference ===&lt;br /&gt;
1. Messer, W., et al., Functional domains of DnaA proteins. Biochimie, 1999. 81(8-9): p. 819-25.&lt;br /&gt;
&lt;br /&gt;
2. Erzberger, J.P., et al., The structure of bacterial DnaA: implications for general mechanisms underlying DNA replication initiation. EMBO J. 2002 Sep 16;21(18):4763-73.&lt;br /&gt;
&lt;br /&gt;
3. Tsodikov OV and Biswas T. Structural and thermodynamic signatures of DNA recognition by Mycobacterium tuberculosis DnaA. J Mol Biol. 2011 Jul 15;410(3):461-76. Epub 2011 May 18.&lt;br /&gt;
&lt;br /&gt;
4. Erzberger, J.P., et al., Structural basis for ATP-dependent DnaA assembly and replication-origin remodeling. Nat Struct Mol Biol. 2006 Aug;13(8):676-83. Epub 2006 Jul 9.&lt;/div&gt;</summary>
		<author><name>Jing Liu</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1543507</id>
		<title>User:Jing Liu/Sandbox 1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1543507"/>
		<updated>2012-10-10T15:38:02Z</updated>

		<summary type="html">&lt;p&gt;Jing Liu: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;One of the [[CBI Molecules]] being studied in the  [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].&lt;br /&gt;
&lt;br /&gt;
==Your Heading Here (maybe something like &#039;Structure&#039;)==&amp;lt;StructureSection load=&#039;1dq8&#039; size=&#039;300&#039; side=&#039;right&#039; caption=&#039;Structure of HMG-CoA reductase (PDB entry [[1dq8]])&#039; scene=&#039;&#039;&amp;gt;Anything in this section will appear adjacent to the 3D structure and will be scrollable.&lt;br /&gt;
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&amp;lt;Structure load=&#039;1L8Q&#039; size=&#039;300&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;1L8Q 76-399&#039; scene=&#039;User:Jing_Liu/Sandbox_1/1/4&#039; /&amp;gt;&lt;br /&gt;
This is a &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/4&#039;&amp;gt;DnaA monomer strucure(residues 76-399)&amp;lt;/scene&amp;gt;, which contains an &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/5&#039;&amp;gt;ADP&amp;lt;/scene&amp;gt; in it.&lt;br /&gt;
&lt;br /&gt;
=== DnaA function in Prokaryotes===&lt;br /&gt;
DnaA is an AAA+ protein in prokaryotes for DNA replication initiation. To ensure correct timing of DNA replication, intracellular DnaA is under multi-level control, including changing expression/degradation level, regulator control and functional activation/inactivation by nucleotide-depedent conformational change. DnaA is a conserved protein in prokaryotes. In &#039;&#039;E. coli&#039;&#039;, There are four regions in this protein[http://www.ncbi.nlm.nih.gov/pubmed/10572294]:&lt;br /&gt;
&lt;br /&gt;
I: residues 1-85. DnaB loading domain;&lt;br /&gt;
&lt;br /&gt;
II: residues 86-133. linker region;&lt;br /&gt;
&lt;br /&gt;
III: residues 134-372. ATPase domain;&lt;br /&gt;
&lt;br /&gt;
IV: residues 373-467. DNA binding domain;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
DnaA function is regulated by different nucleotide binding state. In ATP bound state, DnaA can recognize more binding elements on the chromosome(called DnaA box), and initiate replication by unwinding specific region in the DNA and recruit DnaB helicase. However, after the ATP hydrolysis, DnaA-ADP becomes an inactive protein. This activity change was shown to be associated with its oligomeric assembly state.  &lt;br /&gt;
&lt;br /&gt;
=== DnaA Monomer Structure ===&lt;br /&gt;
The &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/4&#039;&amp;gt;structure of DnaA&amp;lt;/scene&amp;gt; in &#039;&#039;Aquifex aeolicus&#039;&#039; was solved in 2002[http://www.ncbi.nlm.nih.gov/pubmed/12234917?dopt=Abstract], and it contains the linker region, AAA+ domain and DNA binding domain(DBD). The interaction with DNA is through the recognization of a conserved 9 bp DNA recognition sequence (TTA/TTNCACC), and this was shown by the crystal structure of the &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/2/1&#039;&amp;gt;complex&amp;lt;/scene&amp;gt; in &#039;&#039;Mycobacterium tuberculosis&#039;&#039;[http://www.ncbi.nlm.nih.gov/pubmed/21620858?dopt=Abstract]. &lt;br /&gt;
&lt;br /&gt;
=== Distinct Assembly State of DnaA ===&lt;br /&gt;
&amp;lt;Structure load=&#039;1L8Q&#039; size=&#039;300&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;2HCB tetramer&#039; scene=&#039;User:Jing_Liu/Sandbox_1/3/3&#039; /&amp;gt;&lt;br /&gt;
The crystal structure of AMP-PCP-bound DnaA reveals a &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/3/3&#039;&amp;gt;right-handed superhelix&amp;lt;/scene&amp;gt; structure[http://www.ncbi.nlm.nih.gov/pubmed/16829961?dopt=Abstract]. Each monomer contact with another two monomers to form a filamentous structure. The engagement of ATP involved the arginine figure at position 230.&lt;br /&gt;
&lt;br /&gt;
=== Reference ===&lt;br /&gt;
1. Messer, W., et al., Functional domains of DnaA proteins. Biochimie, 1999. 81(8-9): p. 819-25.&lt;br /&gt;
&lt;br /&gt;
2. Erzberger, J.P., et al., The structure of bacterial DnaA: implications for general mechanisms underlying DNA replication initiation. EMBO J. 2002 Sep 16;21(18):4763-73.&lt;br /&gt;
&lt;br /&gt;
3. Tsodikov OV and Biswas T. Structural and thermodynamic signatures of DNA recognition by Mycobacterium tuberculosis DnaA. J Mol Biol. 2011 Jul 15;410(3):461-76. Epub 2011 May 18.&lt;br /&gt;
&lt;br /&gt;
4. Erzberger, J.P., et al., Structural basis for ATP-dependent DnaA assembly and replication-origin remodeling. Nat Struct Mol Biol. 2006 Aug;13(8):676-83. Epub 2006 Jul 9.&lt;/div&gt;</summary>
		<author><name>Jing Liu</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1543499</id>
		<title>User:Jing Liu/Sandbox 1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1543499"/>
		<updated>2012-10-10T15:29:54Z</updated>

		<summary type="html">&lt;p&gt;Jing Liu: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;One of the [[CBI Molecules]] being studied in the  [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].&lt;br /&gt;
&lt;br /&gt;
==Your Heading Here (maybe something like &#039;Structure&#039;)==&amp;lt;StructureSection load=&#039;1dq8&#039; size=&#039;500&#039; side=&#039;right&#039; caption=&#039;Structure of HMG-CoA reductase (PDB entry [[1dq8]])&#039; scene=&#039;&#039;&amp;gt;Anything in this section will appear adjacent to the 3D structure and will be scrollable.&lt;br /&gt;
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&amp;lt;/StructureSection&amp;gt;&lt;br /&gt;
&amp;lt;Structure load=&#039;1L8Q&#039; size=&#039;300&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;1L8Q 76-399&#039; scene=&#039;User:Jing_Liu/Sandbox_1/1/4&#039; /&amp;gt;&lt;br /&gt;
This is a &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/4&#039;&amp;gt;DnaA monomer strucure(residues 76-399)&amp;lt;/scene&amp;gt;, which contains an &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/5&#039;&amp;gt;ADP&amp;lt;/scene&amp;gt; in it.&lt;br /&gt;
&lt;br /&gt;
=== DnaA function in Prokaryotes===&lt;br /&gt;
DnaA is an AAA+ protein in prokaryotes for DNA replication initiation. To ensure correct timing of DNA replication, intracellular DnaA is under multi-level control, including changing expression/degradation level, regulator control and functional activation/inactivation by nucleotide-depedent conformational change. DnaA is a conserved protein in prokaryotes. In &#039;&#039;E. coli&#039;&#039;, There are four regions in this protein[http://www.ncbi.nlm.nih.gov/pubmed/10572294]:&lt;br /&gt;
&lt;br /&gt;
I: residues 1-85. DnaB loading domain;&lt;br /&gt;
&lt;br /&gt;
II: residues 86-133. linker region;&lt;br /&gt;
&lt;br /&gt;
III: residues 134-372. ATPase domain;&lt;br /&gt;
&lt;br /&gt;
IV: residues 373-467. DNA binding domain;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
DnaA function is regulated by different nucleotide binding state. In ATP bound state, DnaA can recognize more binding elements on the chromosome(called DnaA box), and initiate replication by unwinding specific region in the DNA and recruit DnaB helicase. However, after the ATP hydrolysis, DnaA-ADP becomes an inactive protein. This activity change was shown to be associated with its oligomeric assembly state.  &lt;br /&gt;
&lt;br /&gt;
=== DnaA Monomer Structure ===&lt;br /&gt;
The &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/4&#039;&amp;gt;structure of DnaA&amp;lt;/scene&amp;gt; in &#039;&#039;Aquifex aeolicus&#039;&#039; was solved in 2002[http://www.ncbi.nlm.nih.gov/pubmed/12234917?dopt=Abstract], and it contains the linker region, AAA+ domain and DNA binding domain(DBD). The interaction with DNA is through the recognization of a conserved 9 bp DNA recognition sequence (TTA/TTNCACC), and this was shown by the crystal structure of the &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/2/1&#039;&amp;gt;complex&amp;lt;/scene&amp;gt; in &#039;&#039;Mycobacterium tuberculosis&#039;&#039;[http://www.ncbi.nlm.nih.gov/pubmed/21620858?dopt=Abstract]. &lt;br /&gt;
&lt;br /&gt;
=== Distinct Assembly State of DnaA ===&lt;br /&gt;
&amp;lt;Structure load=&#039;1L8Q&#039; size=&#039;300&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;2HCB tetramer&#039; scene=&#039;User:Jing_Liu/Sandbox_1/3/3&#039; /&amp;gt;&lt;br /&gt;
The crystal structure of AMP-PCP-bound DnaA reveals a &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/3/3&#039;&amp;gt;right-handed superhelix&amp;lt;/scene&amp;gt; structure[http://www.ncbi.nlm.nih.gov/pubmed/16829961?dopt=Abstract]. Each monomer contact with another two monomers to form a filamentous structure. The engagement of ATP involved the arginine figure at position 230.&lt;br /&gt;
&lt;br /&gt;
=== Reference ===&lt;br /&gt;
1. Messer, W., et al., Functional domains of DnaA proteins. Biochimie, 1999. 81(8-9): p. 819-25.&lt;br /&gt;
&lt;br /&gt;
2. Erzberger, J.P., et al., The structure of bacterial DnaA: implications for general mechanisms underlying DNA replication initiation. EMBO J. 2002 Sep 16;21(18):4763-73.&lt;br /&gt;
&lt;br /&gt;
3. Tsodikov OV and Biswas T. Structural and thermodynamic signatures of DNA recognition by Mycobacterium tuberculosis DnaA. J Mol Biol. 2011 Jul 15;410(3):461-76. Epub 2011 May 18.&lt;br /&gt;
&lt;br /&gt;
4. Erzberger, J.P., et al., Structural basis for ATP-dependent DnaA assembly and replication-origin remodeling. Nat Struct Mol Biol. 2006 Aug;13(8):676-83. Epub 2006 Jul 9.&lt;/div&gt;</summary>
		<author><name>Jing Liu</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1543496</id>
		<title>User:Jing Liu/Sandbox 1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1543496"/>
		<updated>2012-10-10T15:29:24Z</updated>

		<summary type="html">&lt;p&gt;Jing Liu: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;One of the [[CBI Molecules]] being studied in the  [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].&lt;br /&gt;
&lt;br /&gt;
==Your Heading Here (maybe something like &#039;Structure&#039;)==&amp;lt;StructureSection load=&#039;1dq8&#039; size=&#039;500&#039; side=&#039;right&#039; caption=&#039;Structure of HMG-CoA reductase (PDB entry [[1dq8]])&#039; scene=&#039;&#039;&amp;gt;Anything in this section will appear adjacent to the 3D structure and will be scrollable.&lt;br /&gt;
1&lt;br /&gt;
2&lt;br /&gt;
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&amp;lt;/StructureSection&amp;gt;&lt;br /&gt;
&amp;lt;Structure load=&#039;1L8Q&#039; size=&#039;300&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;1L8Q 76-399&#039; scene=&#039;User:Jing_Liu/Sandbox_1/1/4&#039; /&amp;gt;&lt;br /&gt;
This is a &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/4&#039;&amp;gt;DnaA monomer strucure(residues 76-399)&amp;lt;/scene&amp;gt;, which contains an &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/5&#039;&amp;gt;ADP&amp;lt;/scene&amp;gt; in it.&lt;br /&gt;
&lt;br /&gt;
=== DnaA function in Prokaryotes===&lt;br /&gt;
DnaA is an AAA+ protein in prokaryotes for DNA replication initiation. To ensure correct timing of DNA replication, intracellular DnaA is under multi-level control, including changing expression/degradation level, regulator control and functional activation/inactivation by nucleotide-depedent conformational change. DnaA is a conserved protein in prokaryotes. In &#039;&#039;E. coli&#039;&#039;, There are four regions in this protein[http://www.ncbi.nlm.nih.gov/pubmed/10572294]:&lt;br /&gt;
&lt;br /&gt;
I: residues 1-85. DnaB loading domain;&lt;br /&gt;
&lt;br /&gt;
II: residues 86-133. linker region;&lt;br /&gt;
&lt;br /&gt;
III: residues 134-372. ATPase domain;&lt;br /&gt;
&lt;br /&gt;
IV: residues 373-467. DNA binding domain;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
DnaA function is regulated by different nucleotide binding state. In ATP bound state, DnaA can recognize more binding elements on the chromosome(called DnaA box), and initiate replication by unwinding specific region in the DNA and recruit DnaB helicase. However, after the ATP hydrolysis, DnaA-ADP becomes an inactive protein. This activity change was shown to be associated with its oligomeric assembly state.  &lt;br /&gt;
&lt;br /&gt;
=== DnaA Monomer Structure ===&lt;br /&gt;
The &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/4&#039;&amp;gt;structure of DnaA&amp;lt;/scene&amp;gt; in &#039;&#039;Aquifex aeolicus&#039;&#039; was solved in 2002[http://www.ncbi.nlm.nih.gov/pubmed/12234917?dopt=Abstract], and it contains the linker region, AAA+ domain and DNA binding domain(DBD). The interaction with DNA is through the recognization of a conserved 9 bp DNA recognition sequence (TTA/TTNCACC), and this was shown by the crystal structure of the &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/2/1&#039;&amp;gt;complex&amp;lt;/scene&amp;gt; in &#039;&#039;Mycobacterium tuberculosis&#039;&#039;[http://www.ncbi.nlm.nih.gov/pubmed/21620858?dopt=Abstract]. &lt;br /&gt;
&lt;br /&gt;
=== Distinct Assembly State of DnaA ===&lt;br /&gt;
&amp;lt;Structure load=&#039;1L8Q&#039; size=&#039;300&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;2HCB tetramer&#039; scene=&#039;User:Jing_Liu/Sandbox_1/3/3&#039; /&amp;gt;&lt;br /&gt;
The crystal structure of AMP-PCP-bound DnaA reveals a &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/3/3&#039;&amp;gt;right-handed superhelix&amp;lt;/scene&amp;gt; structure[http://www.ncbi.nlm.nih.gov/pubmed/16829961?dopt=Abstract]. Each monomer contact with another two monomers to form a filamentous structure. The engagement of ATP involved the arginine figure at position 230.&lt;br /&gt;
&lt;br /&gt;
=== Reference ===&lt;br /&gt;
1. Messer, W., et al., Functional domains of DnaA proteins. Biochimie, 1999. 81(8-9): p. 819-25.&lt;br /&gt;
&lt;br /&gt;
2. Erzberger, J.P., et al., The structure of bacterial DnaA: implications for general mechanisms underlying DNA replication initiation. EMBO J. 2002 Sep 16;21(18):4763-73.&lt;br /&gt;
&lt;br /&gt;
3. Tsodikov OV and Biswas T. Structural and thermodynamic signatures of DNA recognition by Mycobacterium tuberculosis DnaA. J Mol Biol. 2011 Jul 15;410(3):461-76. Epub 2011 May 18.&lt;br /&gt;
&lt;br /&gt;
4. Erzberger, J.P., et al., Structural basis for ATP-dependent DnaA assembly and replication-origin remodeling. Nat Struct Mol Biol. 2006 Aug;13(8):676-83. Epub 2006 Jul 9.&lt;/div&gt;</summary>
		<author><name>Jing Liu</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1543493</id>
		<title>User:Jing Liu/Sandbox 1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1543493"/>
		<updated>2012-10-10T15:27:30Z</updated>

		<summary type="html">&lt;p&gt;Jing Liu: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;One of the [[CBI Molecules]] being studied in the  [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].&lt;br /&gt;
&lt;br /&gt;
==Your Heading Here (maybe something like &#039;Structure&#039;)==&amp;lt;StructureSection load=&#039;1dq8&#039; size=&#039;500&#039; side=&#039;right&#039; caption=&#039;Structure of HMG-CoA reductase (PDB entry [[1dq8]])&#039; scene=&#039;&#039;&amp;gt;Anything in this section will appear adjacent to the 3D structure and will be scrollable.&lt;br /&gt;
1&lt;br /&gt;
2&lt;br /&gt;
2&lt;br /&gt;
3&lt;br /&gt;
3&lt;br /&gt;
4&lt;br /&gt;
5&lt;br /&gt;
5&lt;br /&gt;
6&lt;br /&gt;
6&lt;br /&gt;
7&lt;br /&gt;
&amp;lt;/StructureSection&amp;gt;&lt;br /&gt;
&amp;lt;Structure load=&#039;1L8Q&#039; size=&#039;300&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;1L8Q 76-399&#039; scene=&#039;User:Jing_Liu/Sandbox_1/1/4&#039; /&amp;gt;&lt;br /&gt;
This is a &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/4&#039;&amp;gt;DnaA monomer strucure(residues 76-399)&amp;lt;/scene&amp;gt;, which contains an &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/5&#039;&amp;gt;ADP&amp;lt;/scene&amp;gt; in it.&lt;br /&gt;
&lt;br /&gt;
=== DnaA function in Prokaryotes===&lt;br /&gt;
DnaA is an AAA+ protein in prokaryotes for DNA replication initiation. To ensure correct timing of DNA replication, intracellular DnaA is under multi-level control, including changing expression/degradation level, regulator control and functional activation/inactivation by nucleotide-depedent conformational change. DnaA is a conserved protein in prokaryotes. In &#039;&#039;E. coli&#039;&#039;, There are four regions in this protein[http://www.ncbi.nlm.nih.gov/pubmed/10572294]:&lt;br /&gt;
&lt;br /&gt;
I: residues 1-85. DnaB loading domain;&lt;br /&gt;
&lt;br /&gt;
II: residues 86-133. linker region;&lt;br /&gt;
&lt;br /&gt;
III: residues 134-372. ATPase domain;&lt;br /&gt;
&lt;br /&gt;
IV: residues 373-467. DNA binding domain;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
DnaA function is regulated by different nucleotide binding state. In ATP bound state, DnaA can recognize more binding elements on the chromosome(called DnaA box), and initiate replication by unwinding specific region in the DNA and recruit DnaB helicase. However, after the ATP hydrolysis, DnaA-ADP becomes an inactive protein. This activity change was shown to be associated with its oligomeric assembly state.  &lt;br /&gt;
&lt;br /&gt;
=== DnaA Monomer Structure ===&lt;br /&gt;
The &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/4&#039;&amp;gt;structure of DnaA&amp;lt;/scene&amp;gt; in &#039;&#039;Aquifex aeolicus&#039;&#039; was solved in 2002[http://www.ncbi.nlm.nih.gov/pubmed/12234917?dopt=Abstract], and it contains the linker region, AAA+ domain and DNA binding domain(DBD). The interaction with DNA is through the recognization of a conserved 9 bp DNA recognition sequence (TTA/TTNCACC), and this was shown by the crystal structure of the &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/2/1&#039;&amp;gt;complex&amp;lt;/scene&amp;gt; in &#039;&#039;Mycobacterium tuberculosis&#039;&#039;[http://www.ncbi.nlm.nih.gov/pubmed/21620858?dopt=Abstract]. &lt;br /&gt;
&lt;br /&gt;
=== Distinct Assembly State of DnaA ===&lt;br /&gt;
&amp;lt;Structure load=&#039;1L8Q&#039; size=&#039;300&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;2HCB tetramer&#039; scene=&#039;User:Jing_Liu/Sandbox_1/3/3&#039; /&amp;gt;&lt;br /&gt;
The crystal structure of AMP-PCP-bound DnaA reveals a &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/3/3&#039;&amp;gt;right-handed superhelix&amp;lt;/scene&amp;gt; structure[http://www.ncbi.nlm.nih.gov/pubmed/16829961?dopt=Abstract]. Each monomer contact with another two monomers to form a filamentous structure. The engagement of ATP involved the arginine figure at position 230.&lt;br /&gt;
&lt;br /&gt;
=== Reference ===&lt;br /&gt;
1. Messer, W., et al., Functional domains of DnaA proteins. Biochimie, 1999. 81(8-9): p. 819-25.&lt;br /&gt;
&lt;br /&gt;
2. Erzberger, J.P., et al., The structure of bacterial DnaA: implications for general mechanisms underlying DNA replication initiation. EMBO J. 2002 Sep 16;21(18):4763-73.&lt;br /&gt;
&lt;br /&gt;
3. Tsodikov OV and Biswas T. Structural and thermodynamic signatures of DNA recognition by Mycobacterium tuberculosis DnaA. J Mol Biol. 2011 Jul 15;410(3):461-76. Epub 2011 May 18.&lt;br /&gt;
&lt;br /&gt;
4. Erzberger, J.P., et al., Structural basis for ATP-dependent DnaA assembly and replication-origin remodeling. Nat Struct Mol Biol. 2006 Aug;13(8):676-83. Epub 2006 Jul 9.&lt;/div&gt;</summary>
		<author><name>Jing Liu</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1543488</id>
		<title>User:Jing Liu/Sandbox 1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1543488"/>
		<updated>2012-10-10T15:24:08Z</updated>

		<summary type="html">&lt;p&gt;Jing Liu: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;One of the [[CBI Molecules]] being studied in the  [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].&lt;br /&gt;
&lt;br /&gt;
==Your Heading Here (maybe something like &#039;Structure&#039;)==&amp;lt;StructureSection load=&#039;1dq8&#039; size=&#039;500&#039; side=&#039;right&#039; caption=&#039;Structure of HMG-CoA reductase (PDB entry [[1dq8]])&#039; scene=&#039;&#039;&amp;gt;Anything in this section will appear adjacent to the 3D structure and will be scrollable.&amp;lt;/StructureSection&amp;gt;&lt;br /&gt;
&amp;lt;Structure load=&#039;1L8Q&#039; size=&#039;300&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;1L8Q 76-399&#039; scene=&#039;User:Jing_Liu/Sandbox_1/1/4&#039; /&amp;gt;&lt;br /&gt;
This is a &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/4&#039;&amp;gt;DnaA monomer strucure(residues 76-399)&amp;lt;/scene&amp;gt;, which contains an &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/5&#039;&amp;gt;ADP&amp;lt;/scene&amp;gt; in it.&lt;br /&gt;
&lt;br /&gt;
=== DnaA function in Prokaryotes===&lt;br /&gt;
DnaA is an AAA+ protein in prokaryotes for DNA replication initiation. To ensure correct timing of DNA replication, intracellular DnaA is under multi-level control, including changing expression/degradation level, regulator control and functional activation/inactivation by nucleotide-depedent conformational change. DnaA is a conserved protein in prokaryotes. In &#039;&#039;E. coli&#039;&#039;, There are four regions in this protein[http://www.ncbi.nlm.nih.gov/pubmed/10572294]:&lt;br /&gt;
&lt;br /&gt;
I: residues 1-85. DnaB loading domain;&lt;br /&gt;
II: residues 86-133. linker region;&lt;br /&gt;
III: residues 134-372. ATPase domain;&lt;br /&gt;
IV: residues 373-467. DNA binding domain;&lt;br /&gt;
&lt;br /&gt;
DnaA function is regulated by different nucleotide binding state. In ATP bound state, DnaA can recognize more binding elements on the chromosome(called DnaA box), and initiate replication by unwinding specific region in the DNA and recruit DnaB helicase. However, after the ATP hydrolysis, DnaA-ADP becomes an inactive protein. This activity change was shown to be associated with its oligomeric assembly state.  &lt;br /&gt;
&lt;br /&gt;
=== DnaA Monomer Structure ===&lt;br /&gt;
The &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/4&#039;&amp;gt;structure of DnaA&amp;lt;/scene&amp;gt; in &#039;&#039;Aquifex aeolicus&#039;&#039; was solved in 2002[http://www.ncbi.nlm.nih.gov/pubmed/12234917?dopt=Abstract], and it contains the linker region, AAA+ domain and DNA binding domain(DBD). The interaction with DNA is through the recognization of a conserved 9 bp DNA recognition sequence (TTA/TTNCACC), and this was shown by the crystal structure of the &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/2/1&#039;&amp;gt;complex&amp;lt;/scene&amp;gt; in &#039;&#039;Mycobacterium tuberculosis&#039;&#039;[http://www.ncbi.nlm.nih.gov/pubmed/21620858?dopt=Abstract]. &lt;br /&gt;
&lt;br /&gt;
=== Distinct Assembly State of DnaA ===&lt;br /&gt;
&amp;lt;Structure load=&#039;1L8Q&#039; size=&#039;300&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;2HCB tetramer&#039; scene=&#039;User:Jing_Liu/Sandbox_1/3/3&#039; /&amp;gt;&lt;br /&gt;
The crystal structure of AMP-PCP-bound DnaA reveals a &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/3/3&#039;&amp;gt;right-handed superhelix&amp;lt;/scene&amp;gt; structure[http://www.ncbi.nlm.nih.gov/pubmed/16829961?dopt=Abstract]. Each monomer contact with another two monomers to form a filamentous structure. The engagement of ATP involved the arginine figure at position 230.&lt;br /&gt;
&lt;br /&gt;
=== Reference ===&lt;br /&gt;
1. Messer, W., et al., Functional domains of DnaA proteins. Biochimie, 1999. 81(8-9): p. 819-25.&lt;br /&gt;
&lt;br /&gt;
2. Erzberger, J.P., et al., The structure of bacterial DnaA: implications for general mechanisms underlying DNA replication initiation. EMBO J. 2002 Sep 16;21(18):4763-73.&lt;br /&gt;
&lt;br /&gt;
3. Tsodikov OV and Biswas T. Structural and thermodynamic signatures of DNA recognition by Mycobacterium tuberculosis DnaA. J Mol Biol. 2011 Jul 15;410(3):461-76. Epub 2011 May 18.&lt;br /&gt;
&lt;br /&gt;
4. Erzberger, J.P., et al., Structural basis for ATP-dependent DnaA assembly and replication-origin remodeling. Nat Struct Mol Biol. 2006 Aug;13(8):676-83. Epub 2006 Jul 9.&lt;/div&gt;</summary>
		<author><name>Jing Liu</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=CBI_Molecules&amp;diff=1391389</id>
		<title>CBI Molecules</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=CBI_Molecules&amp;diff=1391389"/>
		<updated>2012-05-13T13:48:57Z</updated>

		<summary type="html">&lt;p&gt;Jing Liu: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;These are molecules under study by members of the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program].&lt;br /&gt;
Many of the  molecules we study are featured at the [http://www.molecularplayground.org/ Molecular Playground] (see also [[Molecular Playground|Molecular Playground in Proteopedia]]). Follow the links below to read nontechnical descriptions, in Proteopedia, of these molecules.&lt;br /&gt;
&lt;br /&gt;
UMass CBI Members, add your molecules to the list (which is alphabetical by CBI research mentor); follow the instructions below the list.&lt;br /&gt;
&lt;br /&gt;
It&#039;s great to build on a previous entry, but you must leave the earlier one intact and make a copy that you improve and mark as new.  Later we will retain the new one with a merged author list.&lt;br /&gt;
&lt;br /&gt;
Fall 2011: New entries are due 12/16/11. Please append the designation (new Fall 2011) to your new entries. &lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
==Molecules==&lt;br /&gt;
Bhatia Lab&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Alginate-Fall2011]]&#039;&#039;&#039;, Joe White, David Griffin&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Alginate-Fall2010]]&#039;&#039;&#039;, Joe White, David Griffin&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Poly(ethylene glycol)]]&#039;&#039;&#039;, Erika M. Saffer&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
[http://chamberslab.com/wp/ Chambers Lab]&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Glutamate Receptor]]&#039;&#039;&#039;,  Amanda Hussey, Steve McCarron, Rosie Combs-Bachmann, Mariel Feliciano&lt;br /&gt;
&lt;br /&gt;
[http://openwetware.org/wiki/Chien Chien Lab]&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Hexameric ClpX]]&#039;&#039;&#039;, Joanne Lau &lt;br /&gt;
:: Best CBI Molecule 2011&lt;br /&gt;
&lt;br /&gt;
: New Spring 2012! &#039;&#039;&#039;[[Molecular Playground/DNA replication initiator DnaA]]&#039;&#039;&#039;, Jing Liu&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
Forbes Lab&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/CheR]]&#039;&#039;&#039;,  Miaomin Zhang&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/RBP]]&#039;&#039;&#039;,  Jan Panteli&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/TRAIL]]&#039;&#039;&#039;,  Charley Swofford&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
[http://www.biochem.umass.edu/garman/index.html Garman Lab]&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Human Protective Protein Cathepsin A]]&#039;&#039;&#039;, Yadilette Rivera-Colon&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Human PPCA]]&#039;&#039;&#039;, Nilima Kolli&lt;br /&gt;
&lt;br /&gt;
[http://people.chem.umass.edu/gieraschlab/ Gierasch Lab]&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[CRABP I ( Cellular Retinoic Acid Binding Protein )|Molecular Playground/CRABP I]]&#039;&#039;&#039;, Kristine Faye Pobre, Mylene Ferrolino,Mangai Periasamy&lt;br /&gt;
:: Best Overall CBI Molecule 2010&lt;br /&gt;
&lt;br /&gt;
: NEW FALL 2011!&#039;&#039;&#039;[[Molecular Playground/CRABP I (Cellular Retinoic Acid Binding Protein)]]&#039;&#039;&#039;, Gustavo Elberto Epalza Sanchez&lt;br /&gt;
&lt;br /&gt;
: NEW Fall 2011! &#039;&#039;&#039;[[Molecular_Playground/DHFR]]&#039;&#039;&#039;, Karan Hingorani &lt;br /&gt;
&lt;br /&gt;
[http://people.chem.umass.edu/jhardy/ Hardy Lab]&lt;br /&gt;
&lt;br /&gt;
: New Fall 2011&#039;&#039;&#039; [[Molecular Playground/Caspase-6 and neurodegeneration]]&#039;&#039;&#039;, Kevin Buadlart Dagbay&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Caspase-7 Dynamics]]&#039;&#039;&#039;&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Caspase-9 Regulation]]&#039;&#039;&#039;, Kristen Huber&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Caspase-6 (new)]]&#039;&#039;&#039;, Elih Velazquez&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Influenza A M2 transmembrane domain]]&#039;&#039;&#039;, Samantha Nicholls&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Dengue Virus Protease]]&#039;&#039;&#039;, Muslum Yildiz&lt;br /&gt;
&lt;br /&gt;
Hebert Lab&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Saposin C]]&#039;&#039;&#039;, Abla Tannous&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular_Playground/ERMan1]]&#039;&#039;&#039;,  Johan Sunryd&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
[http://people.biochem.umass.edu/aheuck/aph.html Heuck Lab]&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular_Playground/Pcr H]]&#039;&#039;&#039;,  Fabian Romano&lt;br /&gt;
&lt;br /&gt;
[http://www.chem.umass.edu/people/kaltashovlab/ Kaltashov Lab]&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Velaglucerase]]&#039;&#039;&#039;, Adriana Kita&lt;br /&gt;
&lt;br /&gt;
: New Fall 2011&#039;&#039;&#039; [[Molecular Playground/Transferrin]]&#039;&#039;&#039;, Khaja Muneeruddin&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
Knapp lab&lt;br /&gt;
 &lt;br /&gt;
:&#039;&#039;&#039;[[Molecular Playground/Prolyl Hydroxylase Domain (PHD) Enzyme]]&#039;&#039;&#039;, Cristina Martin&lt;br /&gt;
:: Best CBI Molecule Proteopedia Page 2010&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/FIH]]&#039;&#039;&#039;,  Cornelius Taabazuing, Breanne Holmes, John Hangasky&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
[http://people.chem.umass.edu/mmaroney/ Maroney Lab]&lt;br /&gt;
&lt;br /&gt;
: New Fall 2011!! &#039;&#039;&#039;[[Molecular Playground/CsoR and RcnR]]&#039;&#039;&#039;, Heidi Hu&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
[http://www.chem.umass.edu/~cmartin/ Martin Lab]&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/T7 RNAP Conformations]]&#039;&#039;&#039;, Luis E. Ramirez-Tapia &lt;br /&gt;
:: Best CBI Molecule 2011&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/T7 RNA Polymerase (7 mer int)]]&#039;&#039;&#039;, Ankit Vahia&lt;br /&gt;
&lt;br /&gt;
: NEW Fall 2011! &#039;&#039;&#039;[[Molecular Playground/Human mtRNA pol]]&#039;&#039;&#039;, Ketan Mathavan &lt;br /&gt;
&lt;br /&gt;
Peyton Lab&lt;br /&gt;
: NEW FALL 2011! &#039;&#039;&#039;[[Molecular Playground/C-Raf]]&#039;&#039;&#039;, Thuy Nguyen&lt;br /&gt;
: NEW FALL 2011! &#039;&#039;&#039;[[Molecular Playground/FAK]]&#039;&#039;&#039;, Dannielle Ryman&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
[http://roberts.openwetware.org/ Roberts Lab]&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Taxol]]&#039;&#039;&#039;,  Rohan Patil, Sarah Wilson&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Insulin]]&#039;&#039;&#039;, Whitney Stoppel&lt;br /&gt;
&lt;br /&gt;
[http://www.umass.edu/rotellogroup/ Rotello Lab]&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Reverse transcriptase|Molecular Playground/Reverse Transcriptase]]&#039;&#039;&#039;, Daniel Moyano-Marino&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Pancreatic Lipase]]&#039;&#039;&#039;,  Rui Tang&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular playground/Chymotrypsin]]&#039;&#039;&#039;,  Brad&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Targeting Peptide]]&#039;&#039;&#039;, David Solfiell&lt;br /&gt;
&lt;br /&gt;
Schnarr Lab &lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[6-deoxyerythronolide_B_synthase_(DEBS)|Molecular Playground/6-Deoxyerythronolide B Synthase]]&#039;&#039;&#039;, Tsung-Yi Lin, Jon Amoroso&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/ACP apo]]&#039;&#039;&#039;, Gitanjeli Prasad&lt;br /&gt;
&lt;br /&gt;
Tew Lab&lt;br /&gt;
&lt;br /&gt;
: NEW FALL 2011!! &#039;&#039;&#039;[[Molecular Playground/HIV Tat]]&#039;&#039;&#039;, Brittany deRonde&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
Thayumanavan Lab&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Lysozyme ]]&#039;&#039;&#039;, Daniella Gonzalez&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Beta-galactosidase]]&#039;&#039;&#039;, Judy Ventura&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[User:Krishna Reddy Ragupathi|Molecular Playground/Carbonic Anhydrase]]&#039;&#039;&#039;, Krishna Reddy Raghupathi&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[User:Rami Rajasekhar Reddy|Molecular Playground/Avidin]]&#039;&#039;&#039;, Rami Rajasekar Reddy&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Biotin binding avidin]]&#039;&#039;&#039;, Diego Amado &lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[User:Jiaming Zhuang|Molecular Playground/MMP12]]&#039;&#039;&#039;, Jiaming Zhuang&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039; [[User:Jing Guo|Molecular Playground/Gluconase]]&#039;&#039;&#039;, Jing Guo&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Glutathione Reductase]]&#039;&#039;&#039;, Reuben Chacko&lt;br /&gt;
&lt;br /&gt;
Thayumanavan &amp;amp; Vachet Labs&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Trypsin]]&#039;&#039;&#039;, Gladys Murage&lt;br /&gt;
&lt;br /&gt;
[http://people.chem.umass.edu/thompson/index.html Thompson] &amp;amp; [http://www.chem.umass.edu/~rmweis/weislab/ Weis] Labs&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Bacterial Chemotaxis Receptors]]&#039;&#039;&#039;, Lynmarie K. Thompson, Shiela M. Jones&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/cytoplasmic domain of a serine chemotaxis receptor]]&#039;&#039;&#039;,  Meili Yang&lt;br /&gt;
&lt;br /&gt;
: New Fall 2011 &#039;&#039;&#039;[[Molecular Playground/Cytoplasmic domain of chemoreceptor of Thermotoga maritima]]&#039;&#039;&#039;,  Xuni Li&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
[http://www.chem.umass.edu/~vachet/index.html Vachet Lab]&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular playground/beta 2 microglobulin]]&#039;&#039;&#039;,  Nick Borotto&lt;br /&gt;
:: Best CBI Molecule Jmol scenes 2010&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Myoglobin]]&#039;&#039;&#039;,  Yuping Zhou &lt;br /&gt;
&lt;br /&gt;
:&#039;&#039;&#039;[[Molecular Playground/ Copper-Zinc Superoxide Dismutase]]&#039;&#039;&#039;, Shaynah Browne&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
Other Molecules of interest&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/PcrA Helicase]]&#039;&#039;&#039;, Luis E Ramirez-Tapia, [http://www.chem.umass.edu/~cmartin/ Martin Lab]&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
Other Laboratories&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/YKL-40]]&#039;&#039;&#039;, Ralph A. Francescone III, [http://www.bio.umass.edu/mcb/faculty/Shao.html Shao Lab]&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/BLG|Molecular Playground/β-lactoglobulin]]&#039;&#039;&#039;, Daniel Seeman, Dubin Lab&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/ADAM13]]&#039;&#039;&#039;, Genevieve Abbruzzese, Alfandari Lab&lt;br /&gt;
&lt;br /&gt;
==Instructions==&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;Congratulations to the prize-winning CBI molecules noted above! These also provide great examples to follow. Another prize for best CBI Molecule page and/or scene will be awarded in summer 2012!&#039;&#039;&#039;&lt;br /&gt;
&lt;br /&gt;
Fall 2011: Complete steps 1-4 by 12/1/11, in preparation for the CBI Molecule Workshop.&lt;br /&gt;
&lt;br /&gt;
Choose a molecule that is part of your research project. If someone in your group has already made a page for your research molecule, you can improve on that previous entry. You must leave the previously created page intact and make a copy that you improve and mark as new.  Later we will retain the new one with a merged author list.&lt;br /&gt;
&lt;br /&gt;
1. If you don&#039;t already have one, request a Proteopedia account and log in. If you are new to Proteopedia, click Help in the navigation box on the left to get started.&lt;br /&gt;
&lt;br /&gt;
2. Make yourself a sandbox page in which you will develop your CBI Molecule scene and description  (Enter &amp;quot;User:Your Name/Sandbox 1&amp;quot; (omit quotes) in the search box, then follow instructions to edit this page. See example [[User:Lynmarie K Thompson/Sandbox 1]]). &lt;br /&gt;
&lt;br /&gt;
3. Follow the format of the sample CBI molecule page [[Molecular Playground/Bacterial Chemotaxis Receptors]]. Easiest way to do this is to copy this page (in editing mode), paste it into your sandbox page, keep the first paragraph about CBI molecules, and then edit to describe and display your molecule. Your goal is to make this an interesting, nontechnical description of the molecule. If multiple people in one group work on the same molecule, you can each make different scenes for the same CBI molecule and each describe them on the same proteopedia page. Talk with each other about your plans so you are not duplicating efforts.&lt;br /&gt;
&lt;br /&gt;
4. Add a link to your sandbox page at [[Sandbox_CBI]] (CBI Molecules in Progress).&lt;br /&gt;
&lt;br /&gt;
5. Create an attractive scene for your molecule: use the scene authoring tools in the edit mode to create the view you like, then copy the wiki text into your window.&lt;br /&gt;
&lt;br /&gt;
6. Choose a &amp;quot;green scene&amp;quot; on your Proteopedia page to suggest for display at the Molecular Playground and specify a &amp;quot;banner&amp;quot; which will be projected with the molecule. This should be a short, one-line headline for your scene that includes the name of the molecule and what is important about the scene or the molecule. Remember to design this for the general public, including non-scientists. My example is: &amp;quot;Molecular Playground banner: A bacterial chemotaxis receptor protein used by bacteria to &amp;quot;smell&amp;quot; their environment.&amp;quot;&lt;br /&gt;
&lt;br /&gt;
7. When you are happy with your sandbox page, make yourself a permanent Proteopedia page, which will be editable by others. Enter &amp;quot;Molecular Playground/your molecule&amp;quot; (omit quotes) in the search box, then follow the instructions to create a new page with this title. Copy the content of your sandbox to this new page.&lt;br /&gt;
&lt;br /&gt;
8. When you have finished the final version of your page and scene, edit this CBI Molecules page to add a listing and link for your molecule, following the  examples above, and be sure to mark it as NEW FALL 2011. If you are improving a previously created page, leave the old one intact and make a copy that you improve and mark as new.  Later we will retain the new one with a merged author list. When multiple authors contribute to a Molecular Playground page, please indicate your scene with your initials. Please link the lab names to web pages too.&lt;br /&gt;
&lt;br /&gt;
==Links to HELP pages==&lt;br /&gt;
New [[Help:Getting_Started_in_Proteopedia]] &lt;br /&gt;
&lt;br /&gt;
Videos showing how to use Proteopedia:&lt;br /&gt;
[[Proteopedia:Video_Guide]]&lt;br /&gt;
(Sometimes slow -- if you pause the video and wait awhile it will download and then you can play it without interruptions)&lt;br /&gt;
&lt;br /&gt;
[[Proteopedia:DIY:Scenes|Proteopedia Scenes: Do It Yourself]]&lt;br /&gt;
gives succinct step by step instructions on how to create a molecular scene.&lt;br /&gt;
&lt;br /&gt;
A powerpoint-like set of slides that walks a user through the process of creating a new page and a new molecular scene/green link.&lt;br /&gt;
[http://www.proteopedia.org/wiki/images/1/1b/2009_07_13_Proteopedia_Workshop.pdf Proteopedia Workshop Slides]&lt;br /&gt;
&lt;br /&gt;
[[Proteopedia:Guidelines for Ethical Writing]].&lt;br /&gt;
Please pay attention to the section about images. There are links to examples of images re-used with explicit permission.&lt;br /&gt;
&lt;br /&gt;
For other help resources, click on [[Help:Contents|Help]] in the &#039;&#039;navigation&#039;&#039; box at the upper left of every page in Proteopedia.&lt;/div&gt;</summary>
		<author><name>Jing Liu</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=CBI_Molecules&amp;diff=1391388</id>
		<title>CBI Molecules</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=CBI_Molecules&amp;diff=1391388"/>
		<updated>2012-05-13T13:48:04Z</updated>

		<summary type="html">&lt;p&gt;Jing Liu: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;These are molecules under study by members of the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program].&lt;br /&gt;
Many of the  molecules we study are featured at the [http://www.molecularplayground.org/ Molecular Playground] (see also [[Molecular Playground|Molecular Playground in Proteopedia]]). Follow the links below to read nontechnical descriptions, in Proteopedia, of these molecules.&lt;br /&gt;
&lt;br /&gt;
UMass CBI Members, add your molecules to the list (which is alphabetical by CBI research mentor); follow the instructions below the list.&lt;br /&gt;
&lt;br /&gt;
It&#039;s great to build on a previous entry, but you must leave the earlier one intact and make a copy that you improve and mark as new.  Later we will retain the new one with a merged author list.&lt;br /&gt;
&lt;br /&gt;
Fall 2011: New entries are due 12/16/11. Please append the designation (new Fall 2011) to your new entries. &lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
==Molecules==&lt;br /&gt;
Bhatia Lab&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Alginate-Fall2011]]&#039;&#039;&#039;, Joe White, David Griffin&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Alginate-Fall2010]]&#039;&#039;&#039;, Joe White, David Griffin&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Poly(ethylene glycol)]]&#039;&#039;&#039;, Erika M. Saffer&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
[http://chamberslab.com/wp/ Chambers Lab]&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Glutamate Receptor]]&#039;&#039;&#039;,  Amanda Hussey, Steve McCarron, Rosie Combs-Bachmann, Mariel Feliciano&lt;br /&gt;
&lt;br /&gt;
[http://openwetware.org/wiki/Chien Chien Lab]&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Hexameric ClpX]]&#039;&#039;&#039;, Joanne Lau &lt;br /&gt;
:: Best CBI Molecule 2011&lt;br /&gt;
&lt;br /&gt;
: New Spring 2012&#039;&#039;&#039;[[Molecular Playground/DNA replication initiator DnaA]]&#039;&#039;&#039;, Jing Liu&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
Forbes Lab&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/CheR]]&#039;&#039;&#039;,  Miaomin Zhang&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/RBP]]&#039;&#039;&#039;,  Jan Panteli&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/TRAIL]]&#039;&#039;&#039;,  Charley Swofford&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
[http://www.biochem.umass.edu/garman/index.html Garman Lab]&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Human Protective Protein Cathepsin A]]&#039;&#039;&#039;, Yadilette Rivera-Colon&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Human PPCA]]&#039;&#039;&#039;, Nilima Kolli&lt;br /&gt;
&lt;br /&gt;
[http://people.chem.umass.edu/gieraschlab/ Gierasch Lab]&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[CRABP I ( Cellular Retinoic Acid Binding Protein )|Molecular Playground/CRABP I]]&#039;&#039;&#039;, Kristine Faye Pobre, Mylene Ferrolino,Mangai Periasamy&lt;br /&gt;
:: Best Overall CBI Molecule 2010&lt;br /&gt;
&lt;br /&gt;
: NEW FALL 2011!&#039;&#039;&#039;[[Molecular Playground/CRABP I (Cellular Retinoic Acid Binding Protein)]]&#039;&#039;&#039;, Gustavo Elberto Epalza Sanchez&lt;br /&gt;
&lt;br /&gt;
: NEW Fall 2011! &#039;&#039;&#039;[[Molecular_Playground/DHFR]]&#039;&#039;&#039;, Karan Hingorani &lt;br /&gt;
&lt;br /&gt;
[http://people.chem.umass.edu/jhardy/ Hardy Lab]&lt;br /&gt;
&lt;br /&gt;
: New Fall 2011&#039;&#039;&#039; [[Molecular Playground/Caspase-6 and neurodegeneration]]&#039;&#039;&#039;, Kevin Buadlart Dagbay&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Caspase-7 Dynamics]]&#039;&#039;&#039;&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Caspase-9 Regulation]]&#039;&#039;&#039;, Kristen Huber&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Caspase-6 (new)]]&#039;&#039;&#039;, Elih Velazquez&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Influenza A M2 transmembrane domain]]&#039;&#039;&#039;, Samantha Nicholls&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Dengue Virus Protease]]&#039;&#039;&#039;, Muslum Yildiz&lt;br /&gt;
&lt;br /&gt;
Hebert Lab&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Saposin C]]&#039;&#039;&#039;, Abla Tannous&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular_Playground/ERMan1]]&#039;&#039;&#039;,  Johan Sunryd&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
[http://people.biochem.umass.edu/aheuck/aph.html Heuck Lab]&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular_Playground/Pcr H]]&#039;&#039;&#039;,  Fabian Romano&lt;br /&gt;
&lt;br /&gt;
[http://www.chem.umass.edu/people/kaltashovlab/ Kaltashov Lab]&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Velaglucerase]]&#039;&#039;&#039;, Adriana Kita&lt;br /&gt;
&lt;br /&gt;
: New Fall 2011&#039;&#039;&#039; [[Molecular Playground/Transferrin]]&#039;&#039;&#039;, Khaja Muneeruddin&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
Knapp lab&lt;br /&gt;
 &lt;br /&gt;
:&#039;&#039;&#039;[[Molecular Playground/Prolyl Hydroxylase Domain (PHD) Enzyme]]&#039;&#039;&#039;, Cristina Martin&lt;br /&gt;
:: Best CBI Molecule Proteopedia Page 2010&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/FIH]]&#039;&#039;&#039;,  Cornelius Taabazuing, Breanne Holmes, John Hangasky&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
[http://people.chem.umass.edu/mmaroney/ Maroney Lab]&lt;br /&gt;
&lt;br /&gt;
: New Fall 2011!! &#039;&#039;&#039;[[Molecular Playground/CsoR and RcnR]]&#039;&#039;&#039;, Heidi Hu&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
[http://www.chem.umass.edu/~cmartin/ Martin Lab]&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/T7 RNAP Conformations]]&#039;&#039;&#039;, Luis E. Ramirez-Tapia &lt;br /&gt;
:: Best CBI Molecule 2011&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/T7 RNA Polymerase (7 mer int)]]&#039;&#039;&#039;, Ankit Vahia&lt;br /&gt;
&lt;br /&gt;
: NEW Fall 2011! &#039;&#039;&#039;[[Molecular Playground/Human mtRNA pol]]&#039;&#039;&#039;, Ketan Mathavan &lt;br /&gt;
&lt;br /&gt;
Peyton Lab&lt;br /&gt;
: NEW FALL 2011! &#039;&#039;&#039;[[Molecular Playground/C-Raf]]&#039;&#039;&#039;, Thuy Nguyen&lt;br /&gt;
: NEW FALL 2011! &#039;&#039;&#039;[[Molecular Playground/FAK]]&#039;&#039;&#039;, Dannielle Ryman&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
[http://roberts.openwetware.org/ Roberts Lab]&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Taxol]]&#039;&#039;&#039;,  Rohan Patil, Sarah Wilson&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Insulin]]&#039;&#039;&#039;, Whitney Stoppel&lt;br /&gt;
&lt;br /&gt;
[http://www.umass.edu/rotellogroup/ Rotello Lab]&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Reverse transcriptase|Molecular Playground/Reverse Transcriptase]]&#039;&#039;&#039;, Daniel Moyano-Marino&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Pancreatic Lipase]]&#039;&#039;&#039;,  Rui Tang&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular playground/Chymotrypsin]]&#039;&#039;&#039;,  Brad&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Targeting Peptide]]&#039;&#039;&#039;, David Solfiell&lt;br /&gt;
&lt;br /&gt;
Schnarr Lab &lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[6-deoxyerythronolide_B_synthase_(DEBS)|Molecular Playground/6-Deoxyerythronolide B Synthase]]&#039;&#039;&#039;, Tsung-Yi Lin, Jon Amoroso&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/ACP apo]]&#039;&#039;&#039;, Gitanjeli Prasad&lt;br /&gt;
&lt;br /&gt;
Tew Lab&lt;br /&gt;
&lt;br /&gt;
: NEW FALL 2011!! &#039;&#039;&#039;[[Molecular Playground/HIV Tat]]&#039;&#039;&#039;, Brittany deRonde&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
Thayumanavan Lab&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Lysozyme ]]&#039;&#039;&#039;, Daniella Gonzalez&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Beta-galactosidase]]&#039;&#039;&#039;, Judy Ventura&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[User:Krishna Reddy Ragupathi|Molecular Playground/Carbonic Anhydrase]]&#039;&#039;&#039;, Krishna Reddy Raghupathi&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[User:Rami Rajasekhar Reddy|Molecular Playground/Avidin]]&#039;&#039;&#039;, Rami Rajasekar Reddy&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Biotin binding avidin]]&#039;&#039;&#039;, Diego Amado &lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[User:Jiaming Zhuang|Molecular Playground/MMP12]]&#039;&#039;&#039;, Jiaming Zhuang&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039; [[User:Jing Guo|Molecular Playground/Gluconase]]&#039;&#039;&#039;, Jing Guo&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Glutathione Reductase]]&#039;&#039;&#039;, Reuben Chacko&lt;br /&gt;
&lt;br /&gt;
Thayumanavan &amp;amp; Vachet Labs&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Trypsin]]&#039;&#039;&#039;, Gladys Murage&lt;br /&gt;
&lt;br /&gt;
[http://people.chem.umass.edu/thompson/index.html Thompson] &amp;amp; [http://www.chem.umass.edu/~rmweis/weislab/ Weis] Labs&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Bacterial Chemotaxis Receptors]]&#039;&#039;&#039;, Lynmarie K. Thompson, Shiela M. Jones&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/cytoplasmic domain of a serine chemotaxis receptor]]&#039;&#039;&#039;,  Meili Yang&lt;br /&gt;
&lt;br /&gt;
: New Fall 2011 &#039;&#039;&#039;[[Molecular Playground/Cytoplasmic domain of chemoreceptor of Thermotoga maritima]]&#039;&#039;&#039;,  Xuni Li&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
[http://www.chem.umass.edu/~vachet/index.html Vachet Lab]&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular playground/beta 2 microglobulin]]&#039;&#039;&#039;,  Nick Borotto&lt;br /&gt;
:: Best CBI Molecule Jmol scenes 2010&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Myoglobin]]&#039;&#039;&#039;,  Yuping Zhou &lt;br /&gt;
&lt;br /&gt;
:&#039;&#039;&#039;[[Molecular Playground/ Copper-Zinc Superoxide Dismutase]]&#039;&#039;&#039;, Shaynah Browne&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
Other Molecules of interest&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/PcrA Helicase]]&#039;&#039;&#039;, Luis E Ramirez-Tapia, [http://www.chem.umass.edu/~cmartin/ Martin Lab]&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
Other Laboratories&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/YKL-40]]&#039;&#039;&#039;, Ralph A. Francescone III, [http://www.bio.umass.edu/mcb/faculty/Shao.html Shao Lab]&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/BLG|Molecular Playground/β-lactoglobulin]]&#039;&#039;&#039;, Daniel Seeman, Dubin Lab&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/ADAM13]]&#039;&#039;&#039;, Genevieve Abbruzzese, Alfandari Lab&lt;br /&gt;
&lt;br /&gt;
==Instructions==&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;Congratulations to the prize-winning CBI molecules noted above! These also provide great examples to follow. Another prize for best CBI Molecule page and/or scene will be awarded in summer 2012!&#039;&#039;&#039;&lt;br /&gt;
&lt;br /&gt;
Fall 2011: Complete steps 1-4 by 12/1/11, in preparation for the CBI Molecule Workshop.&lt;br /&gt;
&lt;br /&gt;
Choose a molecule that is part of your research project. If someone in your group has already made a page for your research molecule, you can improve on that previous entry. You must leave the previously created page intact and make a copy that you improve and mark as new.  Later we will retain the new one with a merged author list.&lt;br /&gt;
&lt;br /&gt;
1. If you don&#039;t already have one, request a Proteopedia account and log in. If you are new to Proteopedia, click Help in the navigation box on the left to get started.&lt;br /&gt;
&lt;br /&gt;
2. Make yourself a sandbox page in which you will develop your CBI Molecule scene and description  (Enter &amp;quot;User:Your Name/Sandbox 1&amp;quot; (omit quotes) in the search box, then follow instructions to edit this page. See example [[User:Lynmarie K Thompson/Sandbox 1]]). &lt;br /&gt;
&lt;br /&gt;
3. Follow the format of the sample CBI molecule page [[Molecular Playground/Bacterial Chemotaxis Receptors]]. Easiest way to do this is to copy this page (in editing mode), paste it into your sandbox page, keep the first paragraph about CBI molecules, and then edit to describe and display your molecule. Your goal is to make this an interesting, nontechnical description of the molecule. If multiple people in one group work on the same molecule, you can each make different scenes for the same CBI molecule and each describe them on the same proteopedia page. Talk with each other about your plans so you are not duplicating efforts.&lt;br /&gt;
&lt;br /&gt;
4. Add a link to your sandbox page at [[Sandbox_CBI]] (CBI Molecules in Progress).&lt;br /&gt;
&lt;br /&gt;
5. Create an attractive scene for your molecule: use the scene authoring tools in the edit mode to create the view you like, then copy the wiki text into your window.&lt;br /&gt;
&lt;br /&gt;
6. Choose a &amp;quot;green scene&amp;quot; on your Proteopedia page to suggest for display at the Molecular Playground and specify a &amp;quot;banner&amp;quot; which will be projected with the molecule. This should be a short, one-line headline for your scene that includes the name of the molecule and what is important about the scene or the molecule. Remember to design this for the general public, including non-scientists. My example is: &amp;quot;Molecular Playground banner: A bacterial chemotaxis receptor protein used by bacteria to &amp;quot;smell&amp;quot; their environment.&amp;quot;&lt;br /&gt;
&lt;br /&gt;
7. When you are happy with your sandbox page, make yourself a permanent Proteopedia page, which will be editable by others. Enter &amp;quot;Molecular Playground/your molecule&amp;quot; (omit quotes) in the search box, then follow the instructions to create a new page with this title. Copy the content of your sandbox to this new page.&lt;br /&gt;
&lt;br /&gt;
8. When you have finished the final version of your page and scene, edit this CBI Molecules page to add a listing and link for your molecule, following the  examples above, and be sure to mark it as NEW FALL 2011. If you are improving a previously created page, leave the old one intact and make a copy that you improve and mark as new.  Later we will retain the new one with a merged author list. When multiple authors contribute to a Molecular Playground page, please indicate your scene with your initials. Please link the lab names to web pages too.&lt;br /&gt;
&lt;br /&gt;
==Links to HELP pages==&lt;br /&gt;
New [[Help:Getting_Started_in_Proteopedia]] &lt;br /&gt;
&lt;br /&gt;
Videos showing how to use Proteopedia:&lt;br /&gt;
[[Proteopedia:Video_Guide]]&lt;br /&gt;
(Sometimes slow -- if you pause the video and wait awhile it will download and then you can play it without interruptions)&lt;br /&gt;
&lt;br /&gt;
[[Proteopedia:DIY:Scenes|Proteopedia Scenes: Do It Yourself]]&lt;br /&gt;
gives succinct step by step instructions on how to create a molecular scene.&lt;br /&gt;
&lt;br /&gt;
A powerpoint-like set of slides that walks a user through the process of creating a new page and a new molecular scene/green link.&lt;br /&gt;
[http://www.proteopedia.org/wiki/images/1/1b/2009_07_13_Proteopedia_Workshop.pdf Proteopedia Workshop Slides]&lt;br /&gt;
&lt;br /&gt;
[[Proteopedia:Guidelines for Ethical Writing]].&lt;br /&gt;
Please pay attention to the section about images. There are links to examples of images re-used with explicit permission.&lt;br /&gt;
&lt;br /&gt;
For other help resources, click on [[Help:Contents|Help]] in the &#039;&#039;navigation&#039;&#039; box at the upper left of every page in Proteopedia.&lt;/div&gt;</summary>
		<author><name>Jing Liu</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=Molecular_Playground/DNA_replication_initiator_DnaA&amp;diff=1391387</id>
		<title>Molecular Playground/DNA replication initiator DnaA</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=Molecular_Playground/DNA_replication_initiator_DnaA&amp;diff=1391387"/>
		<updated>2012-05-13T13:45:26Z</updated>

		<summary type="html">&lt;p&gt;Jing Liu: New page: One of the CBI Molecules being studied in the  [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at th...&lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;One of the [[CBI Molecules]] being studied in the  [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&amp;lt;Structure load=&#039;1L8Q&#039; size=&#039;300&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;1L8Q 76-399&#039; scene=&#039;User:Jing_Liu/Sandbox_1/1/4&#039; /&amp;gt;&lt;br /&gt;
This is a &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/4&#039;&amp;gt;DnaA monomer strucure(residues 76-399)&amp;lt;/scene&amp;gt;, which contains an &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/5&#039;&amp;gt;ADP&amp;lt;/scene&amp;gt; in it.&lt;br /&gt;
&lt;br /&gt;
=== DnaA function in Prokaryotes===&lt;br /&gt;
DnaA is an AAA+ protein in prokaryotes for DNA replication initiation. To ensure correct timing of DNA replication, intracellular DnaA is under multi-level control, including changing expression/degradation level, regulator control and functional activation/inactivation by nucleotide-depedent conformational change. DnaA is a conserved protein in prokaryotes. In &#039;&#039;E. coli&#039;&#039;, There are four regions in this protein[http://www.ncbi.nlm.nih.gov/pubmed/10572294]:&lt;br /&gt;
&lt;br /&gt;
I: residues 1-85. DnaB loading domain;&lt;br /&gt;
II: residues 86-133. linker region;&lt;br /&gt;
III: residues 134-372. ATPase domain;&lt;br /&gt;
IV: residues 373-467. DNA binding domain;&lt;br /&gt;
&lt;br /&gt;
DnaA function is regulated by different nucleotide binding state. In ATP bound state, DnaA can recognize more binding elements on the chromosome(called DnaA box), and initiate replication by unwinding specific region in the DNA and recruit DnaB helicase. However, after the ATP hydrolysis, DnaA-ADP becomes an inactive protein. This activity change was shown to be associated with its oligomeric assembly state.  &lt;br /&gt;
&lt;br /&gt;
=== DnaA Monomer Structure ===&lt;br /&gt;
The &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/4&#039;&amp;gt;structure of DnaA&amp;lt;/scene&amp;gt; in &#039;&#039;Aquifex aeolicus&#039;&#039; was solved in 2002[http://www.ncbi.nlm.nih.gov/pubmed/12234917?dopt=Abstract], and it contains the linker region, AAA+ domain and DNA binding domain(DBD). The interaction with DNA is through the recognization of a conserved 9 bp DNA recognition sequence (TTA/TTNCACC), and this was shown by the crystal structure of the &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/2/1&#039;&amp;gt;complex&amp;lt;/scene&amp;gt; in &#039;&#039;Mycobacterium tuberculosis&#039;&#039;[http://www.ncbi.nlm.nih.gov/pubmed/21620858?dopt=Abstract]. &lt;br /&gt;
&lt;br /&gt;
=== Distinct Assembly State of DnaA ===&lt;br /&gt;
&amp;lt;Structure load=&#039;1L8Q&#039; size=&#039;300&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;2HCB tetramer&#039; scene=&#039;User:Jing_Liu/Sandbox_1/3/3&#039; /&amp;gt;&lt;br /&gt;
The crystal structure of AMP-PCP-bound DnaA reveals a &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/3/3&#039;&amp;gt;right-handed superhelix&amp;lt;/scene&amp;gt; structure[http://www.ncbi.nlm.nih.gov/pubmed/16829961?dopt=Abstract]. Each monomer contact with another two monomers to form a filamentous structure. The engagement of ATP involved the arginine figure at position 230.&lt;br /&gt;
&lt;br /&gt;
=== Reference ===&lt;br /&gt;
1. Messer, W., et al., Functional domains of DnaA proteins. Biochimie, 1999. 81(8-9): p. 819-25.&lt;br /&gt;
&lt;br /&gt;
2. Erzberger, J.P., et al., The structure of bacterial DnaA: implications for general mechanisms underlying DNA replication initiation. EMBO J. 2002 Sep 16;21(18):4763-73.&lt;br /&gt;
&lt;br /&gt;
3. Tsodikov OV and Biswas T. Structural and thermodynamic signatures of DNA recognition by Mycobacterium tuberculosis DnaA. J Mol Biol. 2011 Jul 15;410(3):461-76. Epub 2011 May 18.&lt;br /&gt;
&lt;br /&gt;
4. Erzberger, J.P., et al., Structural basis for ATP-dependent DnaA assembly and replication-origin remodeling. Nat Struct Mol Biol. 2006 Aug;13(8):676-83. Epub 2006 Jul 9.&lt;/div&gt;</summary>
		<author><name>Jing Liu</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1391386</id>
		<title>User:Jing Liu/Sandbox 1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1391386"/>
		<updated>2012-05-13T13:37:53Z</updated>

		<summary type="html">&lt;p&gt;Jing Liu: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;One of the [[CBI Molecules]] being studied in the  [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&amp;lt;Structure load=&#039;1L8Q&#039; size=&#039;300&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;1L8Q 76-399&#039; scene=&#039;User:Jing_Liu/Sandbox_1/1/4&#039; /&amp;gt;&lt;br /&gt;
This is a &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/4&#039;&amp;gt;DnaA monomer strucure(residues 76-399)&amp;lt;/scene&amp;gt;, which contains an &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/5&#039;&amp;gt;ADP&amp;lt;/scene&amp;gt; in it.&lt;br /&gt;
&lt;br /&gt;
=== DnaA function in Prokaryotes===&lt;br /&gt;
DnaA is an AAA+ protein in prokaryotes for DNA replication initiation. To ensure correct timing of DNA replication, intracellular DnaA is under multi-level control, including changing expression/degradation level, regulator control and functional activation/inactivation by nucleotide-depedent conformational change. DnaA is a conserved protein in prokaryotes. In &#039;&#039;E. coli&#039;&#039;, There are four regions in this protein[http://www.ncbi.nlm.nih.gov/pubmed/10572294]:&lt;br /&gt;
&lt;br /&gt;
I: residues 1-85. DnaB loading domain;&lt;br /&gt;
II: residues 86-133. linker region;&lt;br /&gt;
III: residues 134-372. ATPase domain;&lt;br /&gt;
IV: residues 373-467. DNA binding domain;&lt;br /&gt;
&lt;br /&gt;
DnaA function is regulated by different nucleotide binding state. In ATP bound state, DnaA can recognize more binding elements on the chromosome(called DnaA box), and initiate replication by unwinding specific region in the DNA and recruit DnaB helicase. However, after the ATP hydrolysis, DnaA-ADP becomes an inactive protein. This activity change was shown to be associated with its oligomeric assembly state.  &lt;br /&gt;
&lt;br /&gt;
=== DnaA Monomer Structure ===&lt;br /&gt;
The &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/4&#039;&amp;gt;structure of DnaA&amp;lt;/scene&amp;gt; in &#039;&#039;Aquifex aeolicus&#039;&#039; was solved in 2002[http://www.ncbi.nlm.nih.gov/pubmed/12234917?dopt=Abstract], and it contains the linker region, AAA+ domain and DNA binding domain(DBD). The interaction with DNA is through the recognization of a conserved 9 bp DNA recognition sequence (TTA/TTNCACC), and this was shown by the crystal structure of the &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/2/1&#039;&amp;gt;complex&amp;lt;/scene&amp;gt; in &#039;&#039;Mycobacterium tuberculosis&#039;&#039;[http://www.ncbi.nlm.nih.gov/pubmed/21620858?dopt=Abstract]. &lt;br /&gt;
&lt;br /&gt;
=== Distinct Assembly State of DnaA ===&lt;br /&gt;
&amp;lt;Structure load=&#039;1L8Q&#039; size=&#039;300&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;2HCB tetramer&#039; scene=&#039;User:Jing_Liu/Sandbox_1/3/3&#039; /&amp;gt;&lt;br /&gt;
The crystal structure of AMP-PCP-bound DnaA reveals a &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/3/3&#039;&amp;gt;right-handed superhelix&amp;lt;/scene&amp;gt; structure[http://www.ncbi.nlm.nih.gov/pubmed/16829961?dopt=Abstract]. Each monomer contact with another two monomers to form a filamentous structure. The engagement of ATP involved the arginine figure at position 230.&lt;br /&gt;
&lt;br /&gt;
=== Reference ===&lt;br /&gt;
1. Messer, W., et al., Functional domains of DnaA proteins. Biochimie, 1999. 81(8-9): p. 819-25.&lt;br /&gt;
&lt;br /&gt;
2. Erzberger, J.P., et al., The structure of bacterial DnaA: implications for general mechanisms underlying DNA replication initiation. EMBO J. 2002 Sep 16;21(18):4763-73.&lt;br /&gt;
&lt;br /&gt;
3. Tsodikov OV and Biswas T. Structural and thermodynamic signatures of DNA recognition by Mycobacterium tuberculosis DnaA. J Mol Biol. 2011 Jul 15;410(3):461-76. Epub 2011 May 18.&lt;br /&gt;
&lt;br /&gt;
4. Erzberger, J.P., et al., Structural basis for ATP-dependent DnaA assembly and replication-origin remodeling. Nat Struct Mol Biol. 2006 Aug;13(8):676-83. Epub 2006 Jul 9.&lt;/div&gt;</summary>
		<author><name>Jing Liu</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1391385</id>
		<title>User:Jing Liu/Sandbox 1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1391385"/>
		<updated>2012-05-13T13:35:38Z</updated>

		<summary type="html">&lt;p&gt;Jing Liu: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;One of the [[CBI Molecules]] being studied in the  [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&amp;lt;Structure load=&#039;1L8Q&#039; size=&#039;300&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;1L8Q 76-399&#039; scene=&#039;User:Jing_Liu/Sandbox_1/1/4&#039; /&amp;gt;&lt;br /&gt;
This is a &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/4&#039;&amp;gt;DnaA monomer strucure(residues 76-399)&amp;lt;/scene&amp;gt;, which contains an &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/5&#039;&amp;gt;ADP&amp;lt;/scene&amp;gt; in it.&lt;br /&gt;
&lt;br /&gt;
=== DnaA function in Prokaryotes===&lt;br /&gt;
DnaA is an AAA+ protein in prokaryotes for DNA replication initiation. To ensure correct timing of DNA replication, intracellular DnaA is under multi-level control, including changing expression/degradation level, regulator control and functional activation/inactivation by nucleotide-depedent conformational change. DnaA is a conserved protein in prokaryotes. In &#039;&#039;E. coli&#039;&#039;, There are four regions in this protein[http://www.ncbi.nlm.nih.gov/pubmed/10572294]:&lt;br /&gt;
&lt;br /&gt;
I: residues 1-85. DnaB loading domain;&lt;br /&gt;
II: residues 86-133. linker region;&lt;br /&gt;
III: residues 134-372. ATPase domain;&lt;br /&gt;
IV: residues 373-467. DNA binding domain;&lt;br /&gt;
&lt;br /&gt;
DnaA function is regulated by different nucleotide binding state. In ATP bound state, DnaA can recognize more binding elements on the chromosome(called DnaA box), and initiate replication by unwinding specific region in the DNA and recruit DnaB helicase. However, after the ATP hydrolysis, DnaA-ADP becomes an inactive protein. This activity change was shown to be associated with its oligomeric assembly state.  &lt;br /&gt;
&lt;br /&gt;
=== DnaA Monomer Structure ===&lt;br /&gt;
The &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/4&#039;&amp;gt;structure of DnaA&amp;lt;/scene&amp;gt; in &#039;&#039;Aquifex aeolicus&#039;&#039; was solved in 2002[http://www.ncbi.nlm.nih.gov/pubmed/12234917?dopt=Abstract], and it contains the linker region, AAA+ domain and DNA binding domain(DBD). The interaction with DNA is through the recognization of a conserved 9 bp DNA recognition sequence (TTA/TTNCACC), and this was shown by the crystal structure of the &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/2/1&#039;&amp;gt;complex&amp;lt;/scene&amp;gt; in &#039;&#039;Mycobacterium tuberculosis&#039;&#039;[http://www.ncbi.nlm.nih.gov/pubmed/21620858?dopt=Abstract]. &lt;br /&gt;
&lt;br /&gt;
=== Distinct Assembly State of DnaA ===&lt;br /&gt;
&amp;lt;Structure load=&#039;1L8Q&#039; size=&#039;300&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;2HCB tetramer&#039; scene=&#039;User:Jing_Liu/Sandbox_1/3/3&#039; /&amp;gt;&lt;br /&gt;
The crystal structure of AMP-PCP-bound DnaA reveals a &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/3/3&#039;&amp;gt;right-handed superhelix&amp;lt;/scene&amp;gt; structure[http://www.ncbi.nlm.nih.gov/pubmed/16829961?dopt=Abstract]. Each monomer contact with another two monomers to form a filamentous structure. The engagement of ATP involved the arginine figure at position 230.&lt;br /&gt;
&lt;br /&gt;
=== Reference ===&lt;br /&gt;
1. Messer, W., et al., Functional domains of DnaA proteins. Biochimie, 1999. 81(8-9): p. 819-25.&lt;br /&gt;
2. Erzberger, J.P., et al., The structure of bacterial DnaA: implications for general mechanisms underlying DNA replication initiation. EMBO J. 2002 Sep 16;21(18):4763-73.&lt;br /&gt;
3. Tsodikov OV and Biswas T. Structural and thermodynamic signatures of DNA recognition by Mycobacterium tuberculosis DnaA. J Mol Biol. 2011 Jul 15;410(3):461-76. Epub 2011 May 18.&lt;br /&gt;
4. Erzberger, J.P., et al., Structural basis for ATP-dependent DnaA assembly and replication-origin remodeling. Nat Struct Mol Biol. 2006 Aug;13(8):676-83. Epub 2006 Jul 9.&lt;/div&gt;</summary>
		<author><name>Jing Liu</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1391384</id>
		<title>User:Jing Liu/Sandbox 1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1391384"/>
		<updated>2012-05-13T13:15:03Z</updated>

		<summary type="html">&lt;p&gt;Jing Liu: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;One of the [[CBI Molecules]] being studied in the  [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&amp;lt;Structure load=&#039;1L8Q&#039; size=&#039;300&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;1L8Q 76-399&#039; scene=&#039;User:Jing_Liu/Sandbox_1/1/4&#039; /&amp;gt;&lt;br /&gt;
This is a &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/4&#039;&amp;gt;DnaA monomer strucure(residues 76-399)&amp;lt;/scene&amp;gt;, which contains an &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/5&#039;&amp;gt;ADP&amp;lt;/scene&amp;gt; in it.&lt;br /&gt;
&lt;br /&gt;
=== DnaA function in Prokaryotes===&lt;br /&gt;
DnaA is an AAA+ protein in prokaryotes for DNA replication initiation. To ensure correct timing of DNA replication, intracellular DnaA is under multi-level control, including changing expression/degradation level, regulator control and functional activation/inactivation by nucleotide-depedent conformational change. DnaA is a conserved protein in prokaryotes. In &#039;&#039;E. coli&#039;&#039;, There are four regions in this protein[http://www.ncbi.nlm.nih.gov/pubmed/10572294]:&lt;br /&gt;
&lt;br /&gt;
I: residues 1-85. DnaB loading domain;&lt;br /&gt;
II: residues 86-133. linker region;&lt;br /&gt;
III: residues 134-372. ATPase domain;&lt;br /&gt;
IV: residues 373-467. DNA binding domain;&lt;br /&gt;
&lt;br /&gt;
DnaA function is regulated by different nucleotide binding state. In ATP bound state, DnaA can recognize more binding elements on the chromosome(called DnaA box), and initiate replication by unwinding specific region in the DNA and recruit DnaB helicase. However, after the ATP hydrolysis, DnaA-ADP becomes an inactive protein. This activity change was shown to be associated with its oligomeric assembly state.  &lt;br /&gt;
&lt;br /&gt;
=== DnaA Monomer Structure ===&lt;br /&gt;
&amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/4&#039;&amp;gt;This structure of DnaA in &#039;&#039;Aquifex aeolicus&#039;&#039;&amp;lt;/scene&amp;gt;  was solved in 2002[http://www.ncbi.nlm.nih.gov/pubmed/12234917?dopt=Abstract], and it contains the linker region, AAA+ domain and DNA binding domain(DBD). The interaction with DNA is through the recognization of a conserved 9 bp DNA recognition sequence (TTA/TTNCACC), and this was shown by the crystal structure of the &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/2/1&#039;&amp;gt;complex&amp;lt;/scene&amp;gt; in &#039;&#039;Mycobacterium tuberculosis&#039;&#039;[http://www.ncbi.nlm.nih.gov/pubmed/21620858?dopt=Abstract]. &lt;br /&gt;
&lt;br /&gt;
=== Distinct Assembly State of DnaA ===&lt;br /&gt;
&lt;br /&gt;
=== Reference ===&lt;/div&gt;</summary>
		<author><name>Jing Liu</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1391383</id>
		<title>User:Jing Liu/Sandbox 1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1391383"/>
		<updated>2012-05-13T12:52:04Z</updated>

		<summary type="html">&lt;p&gt;Jing Liu: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;One of the [[CBI Molecules]] being studied in the  [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&amp;lt;Structure load=&#039;1L8Q&#039; size=&#039;300&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;1L8Q&#039; scene=&#039;User:Jing_Liu/Sandbox_1/1/4&#039; /&amp;gt;&lt;br /&gt;
This is a &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/4&#039;&amp;gt;DnaA monomer strucure(Residues 76-399)&amp;lt;/scene&amp;gt;, which contains an &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/5&#039;&amp;gt;ADP&amp;lt;/scene&amp;gt; in it.&lt;br /&gt;
&lt;br /&gt;
=== DnaA function in Prokaryotes===&lt;br /&gt;
DnaA is an AAA+ protein in prokaryotes for DNA replication initiation. To ensure correct timing of DNA replication, intracellular DnaA is under multi-level control, including changing expression/degradation level, regulator control and functional activation/inactivation by nucleotide-depedent conformational change. DnaA is a conserved protein in prokaryotes. In &#039;&#039;E. coli&#039;&#039;, There are four regions in this protein[http://www.ncbi.nlm.nih.gov/pubmed/10572294]:&lt;br /&gt;
&lt;br /&gt;
I: residues 1-85. DnaB loading domain;&lt;br /&gt;
II: residues 86-133. linker region;&lt;br /&gt;
III: residues 134-372. ATPase domain;&lt;br /&gt;
IV: residues 373-467. DNA binding domain;&lt;br /&gt;
&lt;br /&gt;
DnaA function is regulated by different nucleotide binding state. In ATP bound state, DnaA can recognize more binding elements on the chromosome(called DnaA box), and initiate replication by unwinding specific region in the DNA and recruit DnaB helicase. However, after the ATP hydrolysis, DnaA-ADP becomes an inactive protein. This activity change was shown to be associated with its oligomeric assembly state.  &lt;br /&gt;
&lt;br /&gt;
=== DnaA Monomer Structure ===&lt;br /&gt;
The DnaA monomeric state of &lt;br /&gt;
&lt;br /&gt;
=== Distinct Assembly State of DnaA ===&lt;br /&gt;
&lt;br /&gt;
=== Reference ===&lt;/div&gt;</summary>
		<author><name>Jing Liu</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1391382</id>
		<title>User:Jing Liu/Sandbox 1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1391382"/>
		<updated>2012-05-13T12:43:28Z</updated>

		<summary type="html">&lt;p&gt;Jing Liu: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;One of the [[CBI Molecules]] being studied in the  [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&amp;lt;Structure load=&#039;1L8Q&#039; size=&#039;300&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;1L8Q&#039; scene=&#039;User:Jing_Liu/Sandbox_1/1/4&#039; /&amp;gt;&lt;br /&gt;
This is a &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/4&#039;&amp;gt;DnaA monomer strucure(Residues 76-399)&amp;lt;/scene&amp;gt;, which contains an &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/5&#039;&amp;gt;ADP&amp;lt;/scene&amp;gt; in it.&lt;br /&gt;
&lt;br /&gt;
=== DnaA function in Prokaryotes===&lt;br /&gt;
DnaA is an AAA+ protein in prokaryotes for DNA replication initiation. To ensure correct timing of DNA replication, intracellular DnaA is under multi-level control, including changing expression/degradation level, regulator control and functional activation/inactivation by nucleotide-depedent conformational change. DnaA is a conserved protein in prokaryotes. In &#039;&#039;E. coli&#039;&#039;, There are four regions in this protein:&lt;br /&gt;
&lt;br /&gt;
I: residues 1-85. DnaB loading domain;&lt;br /&gt;
II: residues 86-133. linker region;&lt;br /&gt;
III: residues 134-372. ATPase domain;&lt;br /&gt;
IV: residues 373-467. DNA binding domain;&lt;br /&gt;
&lt;br /&gt;
DnaA function is regulated by different nucleotide binding state. In ATP bound state, DnaA can recognize more binding elements on the chromosome(called DnaA box), and initiate replication by unwinding specific region in the DNA and recruit DnaB helicase. However, after the ATP hydrolysis, DnaA-ADP becomes an inactive protein. This activity change was shown to be associated with its oligomeric assembly state.  &lt;br /&gt;
&lt;br /&gt;
=== DnaA Monomer Structure ===&lt;br /&gt;
&lt;br /&gt;
=== Distinct Assembly State of DnaA ===&lt;br /&gt;
&lt;br /&gt;
=== Reference ===&lt;/div&gt;</summary>
		<author><name>Jing Liu</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1391381</id>
		<title>User:Jing Liu/Sandbox 1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1391381"/>
		<updated>2012-05-13T12:37:04Z</updated>

		<summary type="html">&lt;p&gt;Jing Liu: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;One of the [[CBI Molecules]] being studied in the  [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&amp;lt;Structure load=&#039;1L8Q&#039; size=&#039;300&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;1L8Q&#039; scene=&#039;User:Jing_Liu/Sandbox_1/1/4&#039; /&amp;gt;&lt;br /&gt;
This is a &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/4&#039;&amp;gt;DnaA monomer strucure(Residues 76-399)&amp;lt;/scene&amp;gt;, which contains an &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/5&#039;&amp;gt;ADP&amp;lt;/scene&amp;gt; in it.&lt;br /&gt;
&lt;br /&gt;
=== DnaA function in Prokaryotes===&lt;br /&gt;
DnaA is an AAA+ protein in prokaryotes for DNA replication initiation. To ensure correct timing of DNA replication, intracellular DnaA is under multi-level control, including changing expression/degradation level, regulator control and functional activation/inactivation by nucleotide-depedent conformational change. DnaA is a conserved protein in prokaryotes. In &#039;&#039;E. coli&#039;&#039;, There are four regions in this protein:&lt;br /&gt;
&lt;br /&gt;
I: residues 1-85. DnaB loading domain;&lt;br /&gt;
II: residues 86-133. linker region;&lt;br /&gt;
III: residues 134-372. ATPase domain;&lt;br /&gt;
IV: residues 373-467. DNA binding domain;&lt;br /&gt;
&lt;br /&gt;
=== Process of DNA Replication Initiation ===&lt;br /&gt;
&lt;br /&gt;
=== DnaA Monomer Structure ===&lt;br /&gt;
&lt;br /&gt;
=== Distinct Assembly State of DnaA ===&lt;br /&gt;
&lt;br /&gt;
=== Reference ===&lt;/div&gt;</summary>
		<author><name>Jing Liu</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1391380</id>
		<title>User:Jing Liu/Sandbox 1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1391380"/>
		<updated>2012-05-13T12:29:28Z</updated>

		<summary type="html">&lt;p&gt;Jing Liu: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;One of the [[CBI Molecules]] being studied in the  [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&amp;lt;Structure load=&#039;1L8Q&#039; size=&#039;300&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;1L8Q&#039; scene=&#039;User:Jing_Liu/Sandbox_1/1/4&#039; /&amp;gt;&lt;br /&gt;
This is a &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/4&#039;&amp;gt;DnaA monomer strucure(Residues 76-399)&amp;lt;/scene&amp;gt;, which contains &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/5&#039;&amp;gt;and ADP&amp;lt;/scene&amp;gt; in it.&lt;br /&gt;
&lt;br /&gt;
=== DnaA function in Prokaryotes===&lt;br /&gt;
DnaA is a conserved AAA+protein in prokaryotes for DNA replication initiation. To ensure correct timing of DNA replication, intracellular DnaA is under multi-level control, including changing expression/degradation level, regulator control and functional activation/inactivation by nucleotide-depedent conformational change. &lt;br /&gt;
&lt;br /&gt;
=== Process of DNA Replication Initiation ===&lt;br /&gt;
&lt;br /&gt;
=== DnaA Monomer Structure ===&lt;br /&gt;
&lt;br /&gt;
=== Distinct Assembly State of DnaA ===&lt;br /&gt;
&lt;br /&gt;
=== Reference ===&lt;/div&gt;</summary>
		<author><name>Jing Liu</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1391379</id>
		<title>User:Jing Liu/Sandbox 1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1391379"/>
		<updated>2012-05-13T12:05:43Z</updated>

		<summary type="html">&lt;p&gt;Jing Liu: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;One of the [[CBI Molecules]] being studied in the  [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&amp;lt;Structure load=&#039;1L8Q&#039; size=&#039;300&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;1L8Q&#039; scene=&#039;User:Jing_Liu/Sandbox_1/1/4&#039; /&amp;gt;&lt;br /&gt;
This is a &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/4&#039;&amp;gt;DnaA monomer strucure(Residues 76-399)&amp;lt;/scene&amp;gt;, which contains &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/3&#039;&amp;gt;and ADP&amp;lt;/scene&amp;gt; in it.&lt;br /&gt;
&lt;br /&gt;
=== DnaA function in Prokaryotes===&lt;br /&gt;
DnaA is a conserved AAA+protein in prokaryotes for DNA replication initiation. To ensure correct timing of DNA replication, intracellular DnaA is under multi-level control, including changing expression/degradation level, regulator control and functional activation/inactivation by nucleotide-depedent conformational change. &lt;br /&gt;
&lt;br /&gt;
=== Process of DNA Replication Initiation ===&lt;br /&gt;
&lt;br /&gt;
=== DnaA Monomer Structure ===&lt;br /&gt;
&lt;br /&gt;
=== Distinct Assembly State of DnaA ===&lt;br /&gt;
&lt;br /&gt;
=== Reference ===&lt;/div&gt;</summary>
		<author><name>Jing Liu</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1391365</id>
		<title>User:Jing Liu/Sandbox 1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1391365"/>
		<updated>2012-05-13T05:03:55Z</updated>

		<summary type="html">&lt;p&gt;Jing Liu: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;One of the [[CBI Molecules]] being studied in the  [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&amp;lt;Structure load=&#039;1L8Q&#039; size=&#039;300&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;1L8Q&#039; scene=&#039;User:Jing_Liu/Sandbox_1/1/3&#039; /&amp;gt;&lt;br /&gt;
This is a &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/3&#039;&amp;gt;DnaA monomer strucure(Residues 76-399)&amp;lt;/scene&amp;gt;, which contains &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/2/3&#039;&amp;gt;Zn iron&amp;lt;/scene&amp;gt; in it.&lt;br /&gt;
&lt;br /&gt;
=== DnaA function in Prokaryotes===&lt;br /&gt;
DnaA is a conserved AAA+protein in prokaryotes for DNA replication initiation. To ensure correct timing of DNA replication, intracellular DnaA is under multi-level control, including changing expression/degradation level, regulator control and functional activation/inactivation by nucleotide-depedent conformational change. &lt;br /&gt;
&lt;br /&gt;
=== Process of DNA Replication Initiation ===&lt;br /&gt;
&lt;br /&gt;
=== DnaA Monomer Structure ===&lt;br /&gt;
&lt;br /&gt;
=== Distinct Assembly State of DnaA ===&lt;br /&gt;
&lt;br /&gt;
=== Reference ===&lt;/div&gt;</summary>
		<author><name>Jing Liu</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1391364</id>
		<title>User:Jing Liu/Sandbox 1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1391364"/>
		<updated>2012-05-13T05:01:40Z</updated>

		<summary type="html">&lt;p&gt;Jing Liu: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;One of the [[CBI Molecules]] being studied in the  [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&amp;lt;Structure load=&#039;1L8Q&#039; size=&#039;300&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;1L8Q&#039; scene=&#039;User:Jing_Liu/Sandbox_1/1/3&#039; /&amp;gt;&lt;br /&gt;
This is a &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/1&#039;&amp;gt;LTag helicase domain&amp;lt;/scene&amp;gt; of SV40, which contains &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/3/2&#039;&amp;gt;Zn iron&amp;lt;/scene&amp;gt; in it.&lt;br /&gt;
&lt;br /&gt;
=== DnaA function in Prokaryotes===&lt;br /&gt;
DnaA is a conserved AAA+protein in prokaryotes for DNA replication initiation. To ensure correct timing of DNA replication, intracellular DnaA is under multi-level control, including changing expression/degradation level, regulator control and functional activation/inactivation by nucleotide-depedent conformational change. &lt;br /&gt;
&lt;br /&gt;
=== Process of DNA Replication Initiation ===&lt;br /&gt;
&lt;br /&gt;
=== DnaA Monomer Structure ===&lt;br /&gt;
&lt;br /&gt;
=== Distinct Assembly State of DnaA ===&lt;br /&gt;
&lt;br /&gt;
=== Reference ===&lt;/div&gt;</summary>
		<author><name>Jing Liu</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1391363</id>
		<title>User:Jing Liu/Sandbox 1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1391363"/>
		<updated>2012-05-13T05:01:12Z</updated>

		<summary type="html">&lt;p&gt;Jing Liu: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;One of the [[CBI Molecules]] being studied in the  [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&amp;lt;Structure load=&#039;1L8Q&#039; size=&#039;500&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;1L8Q&#039; scene=&#039;User:Jing_Liu/Sandbox_1/1/3&#039; /&amp;gt;&lt;br /&gt;
This is a &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/1&#039;&amp;gt;LTag helicase domain&amp;lt;/scene&amp;gt; of SV40, which contains &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/3/2&#039;&amp;gt;Zn iron&amp;lt;/scene&amp;gt; in it.&lt;br /&gt;
&lt;br /&gt;
=== DnaA function in Prokaryotes===&lt;br /&gt;
DnaA is a conserved AAA+protein in prokaryotes for DNA replication initiation. To ensure correct timing of DNA replication, intracellular DnaA is under multi-level control, including changing expression/degradation level, regulator control and functional activation/inactivation by nucleotide-depedent conformational change. &lt;br /&gt;
&lt;br /&gt;
=== Process of DNA Replication Initiation ===&lt;br /&gt;
&lt;br /&gt;
=== DnaA Monomer Structure ===&lt;br /&gt;
&lt;br /&gt;
=== Distinct Assembly State of DnaA ===&lt;br /&gt;
&lt;br /&gt;
=== Reference ===&lt;/div&gt;</summary>
		<author><name>Jing Liu</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1391362</id>
		<title>User:Jing Liu/Sandbox 1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1391362"/>
		<updated>2012-05-13T04:55:36Z</updated>

		<summary type="html">&lt;p&gt;Jing Liu: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;One of the [[CBI Molecules]] being studied in the  [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&amp;lt;Structure load=&#039;1L8Q&#039; size=&#039;500&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;1L8Q&#039; scene=&#039;User:Jing_Liu/Sandbox_1/1/1&#039; /&amp;gt;&lt;br /&gt;
This is a &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/1&#039;&amp;gt;LTag helicase domain&amp;lt;/scene&amp;gt; of SV40, which contains &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/3/2&#039;&amp;gt;Zn iron&amp;lt;/scene&amp;gt; in it.&lt;br /&gt;
&lt;br /&gt;
=== DnaA function in Prokaryotes===&lt;br /&gt;
DnaA is a conserved AAA+protein in prokaryotes for DNA replication initiation. To ensure correct timing of DNA replication, intracellular DnaA is under multi-level control, including changing expression/degradation level, regulator control and functional activation/inactivation by nucleotide-depedent conformational change. &lt;br /&gt;
&lt;br /&gt;
=== Process of DNA Replication Initiation ===&lt;br /&gt;
&lt;br /&gt;
=== DnaA Monomer Structure ===&lt;br /&gt;
&lt;br /&gt;
=== Distinct Assembly State of DnaA ===&lt;br /&gt;
&lt;br /&gt;
=== Reference ===&lt;/div&gt;</summary>
		<author><name>Jing Liu</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1391361</id>
		<title>User:Jing Liu/Sandbox 1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1391361"/>
		<updated>2012-05-13T04:54:05Z</updated>

		<summary type="html">&lt;p&gt;Jing Liu: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;One of the [[CBI Molecules]] being studied in the  [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&amp;lt;Structure load=&#039;1SVO&#039; size=&#039;500&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;1SVO&#039; scene=&#039;User:Jing_Liu/Sandbox_1/1/1&#039; /&amp;gt;&lt;br /&gt;
This is a &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/1&#039;&amp;gt;LTag helicase domain&amp;lt;/scene&amp;gt; of SV40, which contains &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/3/2&#039;&amp;gt;Zn iron&amp;lt;/scene&amp;gt; in it.&lt;br /&gt;
&lt;br /&gt;
=== DnaA function in Prokaryotes===&lt;br /&gt;
DnaA is a conserved AAA+protein in prokaryotes for DNA replication initiation. To ensure correct timing of DNA replication, intracellular DnaA is under multi-level control, including changing expression/degradation level, regulator control and functional activation/inactivation by nucleotide-depedent conformational change. &lt;br /&gt;
&lt;br /&gt;
=== Process of DNA Replication Initiation ===&lt;br /&gt;
&lt;br /&gt;
=== DnaA Monomer Structure ===&lt;br /&gt;
&lt;br /&gt;
=== Distinct Assembly State of DnaA ===&lt;br /&gt;
&lt;br /&gt;
=== Reference ===&lt;/div&gt;</summary>
		<author><name>Jing Liu</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1391360</id>
		<title>User:Jing Liu/Sandbox 1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1391360"/>
		<updated>2012-05-13T04:32:17Z</updated>

		<summary type="html">&lt;p&gt;Jing Liu: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;One of the [[CBI Molecules]] being studied in the  [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&amp;lt;Structure load=&#039;1SVO&#039; size=&#039;500&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;1SVO&#039; scene=&#039;User:Jing_Liu/Sandbox_1/1/1&#039; /&amp;gt;&lt;br /&gt;
This is a &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/1&#039;&amp;gt;LTag helicase domain&amp;lt;/scene&amp;gt; of SV40, which contains &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/3/2&#039;&amp;gt;Zn iron&amp;lt;/scene&amp;gt; in it.&lt;br /&gt;
&lt;br /&gt;
=== DnaA function in Eubacteria ===&lt;br /&gt;
&lt;br /&gt;
=== Process of DNA Replication Initiation ===&lt;br /&gt;
&lt;br /&gt;
=== DnaA Monomer Structure ===&lt;br /&gt;
&lt;br /&gt;
=== Distinct Assembly State of DnaA ===&lt;br /&gt;
&lt;br /&gt;
=== Reference ===&lt;/div&gt;</summary>
		<author><name>Jing Liu</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1391359</id>
		<title>User:Jing Liu/Sandbox 1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1391359"/>
		<updated>2012-05-13T04:31:47Z</updated>

		<summary type="html">&lt;p&gt;Jing Liu: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;Structure load=&#039;1SVO&#039; size=&#039;500&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;1SVO&#039; scene=&#039;User:Jing_Liu/Sandbox_1/1/1&#039; /&amp;gt;&lt;br /&gt;
This is a &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/1&#039;&amp;gt;LTag helicase domain&amp;lt;/scene&amp;gt; of SV40, which contains &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/3/2&#039;&amp;gt;Zn iron&amp;lt;/scene&amp;gt; in it.&lt;br /&gt;
&lt;br /&gt;
=== DnaA function in Eubacteria ===&lt;br /&gt;
&lt;br /&gt;
=== Process of DNA Replication Initiation ===&lt;br /&gt;
&lt;br /&gt;
=== DnaA Monomer Structure ===&lt;br /&gt;
&lt;br /&gt;
=== Distinct Assembly State of DnaA ===&lt;br /&gt;
&lt;br /&gt;
=== Reference ===&lt;/div&gt;</summary>
		<author><name>Jing Liu</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1391358</id>
		<title>User:Jing Liu/Sandbox 1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1391358"/>
		<updated>2012-05-13T04:31:18Z</updated>

		<summary type="html">&lt;p&gt;Jing Liu: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;Structure load=&#039;1SVO&#039; size=&#039;500&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;1SVO&#039; scene=&#039;User:Jing_Liu/Sandbox_1/1/1&#039; /&amp;gt;&lt;br /&gt;
This is a &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/1&#039;&amp;gt;LTag helicase domain&amp;lt;/scene&amp;gt; of SV40, which contains &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/3/2&#039;&amp;gt;Zn iron&amp;lt;/scene&amp;gt; in it.&lt;br /&gt;
&lt;br /&gt;
=== DnaA function in Eubacteria ===&lt;br /&gt;
&lt;br /&gt;
=== DnaA Monomer Structure ===&lt;br /&gt;
&lt;br /&gt;
=== Distinct Assembly State of DnaA ===&lt;br /&gt;
&lt;br /&gt;
=== Process of DNA Replication Initiation ===&lt;br /&gt;
&lt;br /&gt;
=== Reference ===&lt;/div&gt;</summary>
		<author><name>Jing Liu</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1391357</id>
		<title>User:Jing Liu/Sandbox 1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1391357"/>
		<updated>2012-05-13T04:30:59Z</updated>

		<summary type="html">&lt;p&gt;Jing Liu: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;Structure load=&#039;1SVO&#039; size=&#039;500&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;1SVO&#039; scene=&#039;User:Jing_Liu/Sandbox_1/1/1&#039; /&amp;gt;&lt;br /&gt;
This is a &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/1&#039;&amp;gt;LTag helicase domain&amp;lt;/scene&amp;gt; of SV40, which contains &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/3/2&#039;&amp;gt;Zn iron&amp;lt;/scene&amp;gt; in it.&lt;br /&gt;
&lt;br /&gt;
=== DnaA function in Eubacteria ===&lt;br /&gt;
&lt;br /&gt;
=== DnaA Monomer Structure ===&lt;br /&gt;
&lt;br /&gt;
=== Distinct Assembly State of DnaA ===&lt;br /&gt;
&lt;br /&gt;
=== Process of DNA Replication Initiation ==&lt;br /&gt;
&lt;br /&gt;
=== Reference ===&lt;/div&gt;</summary>
		<author><name>Jing Liu</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1329696</id>
		<title>User:Jing Liu/Sandbox 1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1329696"/>
		<updated>2011-12-07T18:10:41Z</updated>

		<summary type="html">&lt;p&gt;Jing Liu: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;Structure load=&#039;1SVO&#039; size=&#039;500&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;1SVO&#039; scene=&#039;User:Jing_Liu/Sandbox_1/1/1&#039; /&amp;gt;&lt;br /&gt;
This is a &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/1&#039;&amp;gt;LTag helicase domain&amp;lt;/scene&amp;gt; of SV40, which contains &amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/3/2&#039;&amp;gt;Zn iron&amp;lt;/scene&amp;gt; in it.&lt;/div&gt;</summary>
		<author><name>Jing Liu</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1329666</id>
		<title>User:Jing Liu/Sandbox 1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1329666"/>
		<updated>2011-12-07T18:01:16Z</updated>

		<summary type="html">&lt;p&gt;Jing Liu: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;Structure load=&#039;1SVO&#039; size=&#039;500&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;1SVO&#039; scene=&#039;User:Jing_Liu/Sandbox_1/1/1&#039; /&amp;gt;&lt;br /&gt;
&amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/1&#039;&amp;gt;Original view&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/3/1&#039;&amp;gt;Second view&amp;lt;/scene&amp;gt;&lt;/div&gt;</summary>
		<author><name>Jing Liu</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1329665</id>
		<title>User:Jing Liu/Sandbox 1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1329665"/>
		<updated>2011-12-07T18:00:58Z</updated>

		<summary type="html">&lt;p&gt;Jing Liu: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;Structure load=&#039;1SVO&#039; size=&#039;500&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;1SVO&#039; scene=&#039;User:Jing_Liu/Sandbox_1/1/1&#039; /&amp;gt;&lt;br /&gt;
&amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/1&#039;&amp;gt;original view&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/3/1&#039;&amp;gt;Second view&amp;lt;/scene&amp;gt;&lt;/div&gt;</summary>
		<author><name>Jing Liu</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1329662</id>
		<title>User:Jing Liu/Sandbox 1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1329662"/>
		<updated>2011-12-07T18:00:34Z</updated>

		<summary type="html">&lt;p&gt;Jing Liu: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;Structure load=&#039;1SVO&#039; size=&#039;500&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;1SVO&#039; scene=&#039;User:Jing_Liu/Sandbox_1/1/1&#039; /&amp;gt;&lt;br /&gt;
&amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/1/1&#039;&amp;gt;original view&amp;lt;/scene&amp;gt;&lt;br /&gt;
&amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/3/1&#039;&amp;gt;Second view&amp;lt;/scene&amp;gt;&lt;/div&gt;</summary>
		<author><name>Jing Liu</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1329660</id>
		<title>User:Jing Liu/Sandbox 1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1329660"/>
		<updated>2011-12-07T17:59:55Z</updated>

		<summary type="html">&lt;p&gt;Jing Liu: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;Structure load=&#039;1SVO&#039; size=&#039;500&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;original&#039; scene=&#039;User:Jing_Liu/Sandbox_1/1/1&#039; /&amp;gt;&lt;br /&gt;
&amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/3/1&#039;&amp;gt;Second view&amp;lt;/scene&amp;gt;&lt;/div&gt;</summary>
		<author><name>Jing Liu</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1329658</id>
		<title>User:Jing Liu/Sandbox 1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1329658"/>
		<updated>2011-12-07T17:59:39Z</updated>

		<summary type="html">&lt;p&gt;Jing Liu: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;Structure load=&#039;1SVO&#039; size=&#039;500&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;original&#039; scene=&#039;User:Jing_Liu/Sandbox_1/1/1&#039; /&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&amp;lt;Structure load=&#039;1SVO&#039; size=&#039;500&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;rotated&#039; scene=&#039;User:Jing_Liu/Sandbox_1/3/1&#039; /&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Jing_Liu/Sandbox_1/3/1&#039;&amp;gt;Second view&amp;lt;/scene&amp;gt;&lt;/div&gt;</summary>
		<author><name>Jing Liu</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1329632</id>
		<title>User:Jing Liu/Sandbox 1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1329632"/>
		<updated>2011-12-07T17:52:52Z</updated>

		<summary type="html">&lt;p&gt;Jing Liu: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;Structure load=&#039;1SVO&#039; size=&#039;500&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;original&#039; scene=&#039;User:Jing_Liu/Sandbox_1/1/1&#039; /&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;Structure load=&#039;1SVO&#039; size=&#039;500&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;rotated&#039; scene=&#039;User:Jing_Liu/Sandbox_1/3/1&#039; /&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;Structure load=&#039;1SVO&#039; size=&#039;500&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;1SVO&#039; scene=&#039;4&#039; /&amp;gt;&lt;/div&gt;</summary>
		<author><name>Jing Liu</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1329628</id>
		<title>User:Jing Liu/Sandbox 1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1329628"/>
		<updated>2011-12-07T17:50:59Z</updated>

		<summary type="html">&lt;p&gt;Jing Liu: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;Structure load=&#039;1SVO&#039; size=&#039;500&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;original&#039; scene=&#039;User:Jing_Liu/Sandbox_1/2222/1&#039; /&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;Structure load=&#039;1SVO&#039; size=&#039;500&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;rotated&#039; scene=&#039;User:Jing_Liu/Sandbox_1/3/1&#039; /&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;Structure load=&#039;1SVO&#039; size=&#039;500&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;1SVO&#039; scene=&#039;4&#039; /&amp;gt;&lt;/div&gt;</summary>
		<author><name>Jing Liu</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1329627</id>
		<title>User:Jing Liu/Sandbox 1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1329627"/>
		<updated>2011-12-07T17:50:34Z</updated>

		<summary type="html">&lt;p&gt;Jing Liu: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;Structure load=&#039;1SVO&#039; size=&#039;500&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;1SVO&#039; scene=&#039;User:Jing_Liu/Sandbox_1/2222/1&#039; /&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;Structure load=&#039;1SVO&#039; size=&#039;500&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;1SVO&#039; scene=&#039;User:Jing_Liu/Sandbox_1/3/1&#039; /&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;Structure load=&#039;1SVO&#039; size=&#039;500&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;1SVO&#039; scene=&#039;4&#039; /&amp;gt;&lt;/div&gt;</summary>
		<author><name>Jing Liu</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1329625</id>
		<title>User:Jing Liu/Sandbox 1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1329625"/>
		<updated>2011-12-07T17:50:01Z</updated>

		<summary type="html">&lt;p&gt;Jing Liu: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;Structure load=&#039;1SVO&#039; size=&#039;500&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;1SVO&#039; scene=&#039;User:Jing_Liu/Sandbox_1/2222/1&#039; /&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;Structure load=&#039;1SVO&#039; size=&#039;500&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;1SVO&#039; scene=&#039;User:Jing_Liu/Sandbox_1/3/3&#039; /&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;Structure load=&#039;1SVO&#039; size=&#039;500&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;1SVO&#039; scene=&#039;4&#039; /&amp;gt;&lt;/div&gt;</summary>
		<author><name>Jing Liu</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1329623</id>
		<title>User:Jing Liu/Sandbox 1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1329623"/>
		<updated>2011-12-07T17:49:35Z</updated>

		<summary type="html">&lt;p&gt;Jing Liu: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;Structure load=&#039;1SVO&#039; size=&#039;500&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;1SVO&#039; scene=&#039;User:Jing_Liu/Sandbox_1/2222/1&#039; /&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;Structure load=&#039;1SVO&#039; size=&#039;500&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;1SVO&#039; scene=&#039;3&#039; /&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;Structure load=&#039;1SVO&#039; size=&#039;500&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;1SVO&#039; scene=&#039;4&#039; /&amp;gt;&lt;/div&gt;</summary>
		<author><name>Jing Liu</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1329614</id>
		<title>User:Jing Liu/Sandbox 1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1329614"/>
		<updated>2011-12-07T17:47:35Z</updated>

		<summary type="html">&lt;p&gt;Jing Liu: 1&lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;Structure load=&#039;1SVO&#039; size=&#039;500&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;1SVO&#039; scene=&#039;2222&#039; /&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;Structure load=&#039;1SVO&#039; size=&#039;500&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;1SVO&#039; scene=&#039;3&#039; /&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;Structure load=&#039;1SVO&#039; size=&#039;500&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;1SVO&#039; scene=&#039;4&#039; /&amp;gt;&lt;/div&gt;</summary>
		<author><name>Jing Liu</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1329577</id>
		<title>User:Jing Liu/Sandbox 1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1329577"/>
		<updated>2011-12-07T17:39:13Z</updated>

		<summary type="html">&lt;p&gt;Jing Liu: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;Structure load=&#039;1SVO&#039; size=&#039;500&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;1SVO&#039; scene=&#039;Insert optional scene name here&#039; /&amp;gt;&lt;/div&gt;</summary>
		<author><name>Jing Liu</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1329573</id>
		<title>User:Jing Liu/Sandbox 1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1329573"/>
		<updated>2011-12-07T17:38:25Z</updated>

		<summary type="html">&lt;p&gt;Jing Liu: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;Structure load=&#039;1SVO&#039; size=&#039;500&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;Insert caption here&#039; scene=&#039;1SVO&#039; /&amp;gt;hahaha&lt;/div&gt;</summary>
		<author><name>Jing Liu</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1329567</id>
		<title>User:Jing Liu/Sandbox 1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1329567"/>
		<updated>2011-12-07T17:37:48Z</updated>

		<summary type="html">&lt;p&gt;Jing Liu: Replacing page with &amp;#039;&amp;lt;Structure load=&amp;#039;1SVO&amp;#039; size=&amp;#039;500&amp;#039; frame=&amp;#039;true&amp;#039; align=&amp;#039;right&amp;#039; caption=&amp;#039;Insert caption here&amp;#039; scene=&amp;#039;Insert optional scene name here&amp;#039; /&amp;gt;hahaha&amp;#039;&lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;Structure load=&#039;1SVO&#039; size=&#039;500&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;Insert caption here&#039; scene=&#039;Insert optional scene name here&#039; /&amp;gt;hahaha&lt;/div&gt;</summary>
		<author><name>Jing Liu</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1329566</id>
		<title>User:Jing Liu/Sandbox 1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1329566"/>
		<updated>2011-12-07T17:36:50Z</updated>

		<summary type="html">&lt;p&gt;Jing Liu: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;Structure load=&#039;1SVO&#039; size=&#039;500&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;Insert caption here&#039; scene=&#039;Insert optional scene name here&#039; /&amp;gt;[[[[Green Fluorescent Protein]]]]&amp;lt;applet load=&#039;1ema&#039; size=&#039;450&#039; frame=&#039;true&#039; align=&#039;right&#039; scene=&#039;Green_Fluorescent_Protein/1ema_gfp_default/2&#039; caption=&#039;Green fluorescent protein complex with peptide-derived chromophore ([[1ema]])&#039; /&amp;gt; &lt;br /&gt;
&#039;&#039;&#039;Green fluorescent protein (GFP)&#039;&#039;&#039; is a [[bioluminescent]] polypeptide consisting of 238 residues isolated from the body of [[Aequorea victoria]] jellyfish.&amp;lt;ref name=&amp;quot;PDBsum&amp;quot;&amp;gt;[http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=1ema&amp;amp;template=main.html], Protein Database (PDBsum): 1ema.  European Bioinformatics (EBI); 2009.&amp;lt;/ref&amp;gt; GFP converts the blue chemiluminescent of [[aequorin]] in the jellyfish into green fluorescent light.&amp;lt;ref name=&amp;quot;Yang&amp;quot;&amp;gt;[http://www-bioc.rice.edu/Bioch/Phillips/Papers/gfpbio.html], Yang F, Moss LG, Phillips GN Jr.  1996.  The molecular structure of green fluorescent protein.  Biotechnology.  14: 1246-1251.  DOI 10.1038/nbt1096-1246.&amp;lt;/ref&amp;gt; It remains unclear why these jellyfish use fluorescence, why green is better than blue, or why they produce a separate protein for green fluorescence as opposed to simply mutating the present aequorin to shift its wavelength,&amp;lt;ref name=&amp;quot;Tsien&amp;quot; /&amp;gt; but in the laboratory, GFP can be incorporated into a variety of biological systems in order to function as a marker protein. Since its discovery in 1962, GFP has become a significant contributor to the research of monitoring gene expression, localization, mobility, traffic, interactions between various membrane and cytoplasmic proteins, as well as many others.&amp;lt;ref name=&amp;quot;Haldar&amp;quot;&amp;gt;[http://www.springerlink.com/content/wvg513864266g77n/fulltext.pdf], Haldar S, Chattopadhyay A.  2009.  The green journey.  J Fluoresc.  19:1-2.  DOI 10.1007/s10895-008-0455-6; biographical background on [http://en.wikipedia.org/wiki/Douglas_Prasher Douglas Prasher], [http://en.wikipedia.org/wiki/Martin_Chalfie Martin Chalfie] and [http://en.wikipedia.org/wiki/Roger_Tsien Roger Tsien].&amp;lt;/ref&amp;gt;&lt;br /&gt;
&lt;br /&gt;
==History==&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;Aequorea victoria&#039;&#039; was first discovered and investigated for its bioluminescence by Frank Johnson, who invited Osamu Shimomura to work with him in on a small island not far from British Columbia, where the jellyfish is abundant.&amp;lt;ref name=&amp;quot;Shimomura&amp;quot;&amp;gt;[http://nobelprize.org/nobel_prizes/chemistry/laureates/2008/shimomura_lecture.pdf], Shimomura O.  The discovery of green fluorescent protein.  Nobel Prize Lecture; 2009;; biographical background at [http://en.wikipedia.org/wiki/Osamu_Shimomura Wikipedia].&amp;lt;/ref&amp;gt; Found off the west coast of the United States between British Columbia and central California,&amp;lt;ref name=&amp;quot;Cowles&amp;quot;&amp;gt;[http://www.wallawalla.edu/academics/departments/biology/rosario/inverts/Cnidaria/Class-Hydrozoa/Hydromedusae/Aequorea_victoria.html],Cowles D, Cowles J.  &#039;&#039;Aequorea victoria&#039;&#039;.  2007.  Walla Wall University.&amp;lt;/ref&amp;gt; the jellyfish was considered a local phenomenon as it would drift in and out of the harbors.&amp;lt;ref name=&amp;quot;Shimomura&amp;quot; /&amp;gt;&lt;br /&gt;
[[Image:GFP mice.png|thumb|left|450x200px|Mice with GFP inserted into their genomes for neurology studies.]]&lt;br /&gt;
&lt;br /&gt;
Shimomura was originally looking only to isolate the blue luminescent protein of &#039;&#039;Aequorea victoria&#039;&#039;, traditionally thought to be [[luciferase]], but it would soon become apparent that the glow was in fact due to aequorin, a substance related, but slightly varying from luciferase.&amp;lt;ref name=&amp;quot;Haldar&amp;quot; /&amp;gt;&amp;lt;ref name=&amp;quot;Shimomura&amp;quot; /&amp;gt; However, the light emitted from aequorin still differed from the light emitted from the wild jellyfish. This quandary led to the discovery of the green fluorescent protein responsible for this disparity, but sufficient amounts of the protein could not be collected for study until 1979. The journey to discover the nature of GFP had begun.&amp;lt;ref name=&amp;quot;Shimomura&amp;quot; /&amp;gt;&lt;br /&gt;
&lt;br /&gt;
In the 1990’s, Douglas Prasher, Frank Predergast, and co-workers successfully cloned the gene that encoded for GFP.  Martin Chalfie further pursued this line of work and was eventually able to express GFP in heterologous systems such as E. coli and C. elegans.  Chalfie’s research provided the first evidence that GFP was unique as it did not require the presence of any exogenous substance or cofactor for fluorescence.&amp;lt;ref name=&amp;quot;Haldar&amp;quot; /&amp;gt; The lack for the need for a cofactor proved that the cloned GFP gene contained all the information necessary for posttranslational synthesis of the chromophore. &amp;lt;ref name=&amp;quot;Tsien&amp;quot; /&amp;gt;&lt;br /&gt;
&lt;br /&gt;
Roger Tsien and co-workers were intrigued by the absence of a necessary cofactor and began to research the structure of GFP and how it relates to its fluorescence.  They discovered that a helix within the beta barrel structure of GFP actually contained a fluorophore responsible for fluorescence.  In researching its structure, they were able to develop GFP derivatives with improved fluorescence and photo-stability.  Shimomura, Chalfie, and Tsien were each recognized for their work involving GFP with the Nobel Prize in 2008.&amp;lt;ref name=&amp;quot;Haldar&amp;quot; /&amp;gt;  In the time since the work of these three researchers, GFP has been successfully expressed and utilized in bacteria, yeast, slime mold, plants, drosophila fruit flies, zebra-fish, and mammalian cells.&amp;lt;ref name=&amp;quot;Yang&amp;quot; /&amp;gt;  Below, mice have had GFP inserted into their genomes for studies in neurology.&lt;br /&gt;
&lt;br /&gt;
==Structure==&lt;br /&gt;
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===Primary &amp;amp; Secondary Structure===&lt;br /&gt;
{{STRUCTURE_1ema |  SIZE=400 |PDB=1ema  |  SCENE=Green_Fluorescent_Protein/1ema_gfp_default/2 |CAPTION = 1ema, resolution 1.90&amp;amp;Aring; (&amp;lt;scene name=&#039;Green_Fluorescent_Protein/1ema_gfp_default/2&#039;&amp;gt;default scene&amp;lt;/scene&amp;gt;).}}&lt;br /&gt;
Green fluorescent protein (&amp;lt;scene name=&#039;Green_Fluorescent_Protein/1ema_gfp_default/2&#039;&amp;gt;default scene&amp;lt;/scene&amp;gt;) is a 21 kDa protein consisting of 238 residues strung together&amp;lt;ref&amp;gt;Primary structure at [http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=1ema&amp;amp;template=protein.html&amp;amp;r=wiring&amp;amp;l=1&amp;amp;chain=A www.ebi.aci.uk].&amp;lt;/ref&amp;gt; to form a  &lt;br /&gt;
&amp;lt;scene name=&#039;Green_Fluorescent_Protein/1ema_gfp_barrel/2&#039;&amp;gt;secondary structure&amp;lt;/scene&amp;gt; of five α-helices and one eleven-stranded β-pleated sheet,&amp;lt;ref name=&amp;quot;PDBsum&amp;quot; /&amp;gt; where each strand contains nine to thirteen residues each.&amp;lt;ref name=&amp;quot;Ormo&amp;quot; /&amp;gt;  (To view the primary and secondary structure of GFP, go to .)  These β-strands display an almost “seamless symmetry” in which only two of the strands vary in structural content.&amp;lt;ref name=&amp;quot;Phillips&amp;quot;&amp;gt;PMID: 9434902&amp;lt;/ref&amp;gt;  This β-sheet conforms itself through regular hydrogen bonding into a β-barrel.&amp;lt;ref name=&amp;quot;Yang&amp;quot; /&amp;gt;  In GFP, the structure is so regular that &amp;lt;scene name=&#039;Green_Fluorescent_Protein/Water_stripes/1&#039;&amp;gt;&amp;quot;stripes&amp;quot;&amp;lt;/scene&amp;gt; of water molecules (red) can be seen following the structure of the barrel.&amp;lt;ref name=&amp;quot;Phillips&amp;quot; /&amp;gt;  Together with the α-helices at either end of the molecule, a nearly perfect cylinder is produced, 42Å long and 24Å in diameter,&amp;lt;ref name=&amp;quot;Ormo&amp;quot; /&amp;gt; creating what is referred to as a “β-can” formation.&amp;lt;ref name=&amp;quot;Phillips&amp;quot; /&amp;gt;  The short helical segments at either end of the cylinder form “caps” to further protect the interior of the β-barrel.&amp;lt;ref name=&amp;quot;Phillips&amp;quot; /&amp;gt;  Overall stability is maintained by this β-can structure, helping to resist unfolding from heat and other denaturants.&amp;lt;ref name=&amp;quot;Yang&amp;quot; /&amp;gt;&lt;br /&gt;
&lt;br /&gt;
One &amp;lt;scene name=&#039;Green_Fluorescent_Protein/Central_helix/1&#039;&amp;gt;α-helix&amp;lt;/scene&amp;gt; can be found running through the central axis of the β-barrel,&amp;lt;ref name=&amp;quot;Haldar&amp;quot; /&amp;gt; roughly &amp;lt;scene name=&#039;Green_Fluorescent_Protein/Perpendicular/1&#039;&amp;gt;perpendicular&amp;lt;/scene&amp;gt; to the symmetry axis of the barrel.&amp;lt;ref name=&amp;quot;Ormo&amp;quot;&amp;gt;Ormo M, Cubitt AB, Kallio K, Gross LA, Tsien RY, Remington SJ.  1996.  Crystal structure of the &#039;&#039;Aequorea victoria&#039;&#039; green fluorescent protein.  Science.  273(5280):1392-1395.  DOI 10.1126/science.273.5280.1392.&amp;lt;/ref&amp;gt;  This helix is extremely important as it contains the fluorophore responsible for fluorescence.&amp;lt;ref name=&amp;quot;Yang&amp;quot; /&amp;gt;&amp;lt;ref name=&amp;quot;Haldar&amp;quot; /&amp;gt;  This α-helix in particular is highly stabilized by the many &amp;lt;scene name=&#039;Green_Fluorescent_Protein/Spacefill/1&#039;&amp;gt;contacts&amp;lt;/scene&amp;gt; that are made with each strand of the barrel.&amp;lt;ref name=&amp;quot;Andrews&amp;quot;&amp;gt;PMID:18713871&amp;lt;/ref&amp;gt;&lt;br /&gt;
&lt;br /&gt;
{{Link Toggle FancyCartoonHighQualityView}}.&lt;br /&gt;
&lt;br /&gt;
===The Chromophore===&lt;br /&gt;
&lt;br /&gt;
The &amp;lt;scene name=&#039;Green_Fluorescent_Protein/Chromophore/1&#039;&amp;gt;chromophore&amp;lt;/scene&amp;gt; (&amp;lt;scene name=&#039;Green_Fluorescent_Protein/1ema_gfp_chromophorezoom/6&#039;&amp;gt;top view&amp;lt;/scene&amp;gt;) of GFP is located at the center of the β-barrel with a wild-type excitation peak of 395 nm, and a minor peak at 475 nm (about three times less intense&amp;lt;ref name=&amp;quot;Tsien&amp;quot; /&amp;gt;) &amp;lt;ref name=&amp;quot;Yang&amp;quot; /&amp;gt;&amp;lt;ref name=&amp;quot;Cubitt&amp;quot; /&amp;gt;&amp;lt;ref name=&amp;quot;Ormo&amp;quot; /&amp;gt;&amp;lt;ref name=&amp;quot;Phillips&amp;quot; /&amp;gt; with extinction coefficients of approximately 30,000 and 7,000 M&amp;lt;sup&amp;gt;-1&amp;lt;/sup&amp;gt; cm&amp;lt;sup&amp;gt;-1&amp;lt;/sup&amp;gt;, respectively.&amp;lt;ref name=&amp;quot;Yang&amp;quot; /&amp;gt;&amp;lt;ref name=&amp;quot;Phillips&amp;quot; /&amp;gt;  Interestingly, the &#039;&#039;Aequorea victoria&#039;&#039; jellyfish utilizes the smaller of the two excitation peaks as pure aequorin emits a light of 470 nm.&amp;lt;ref name=&amp;quot;Tsien&amp;quot;&amp;gt;Tsien, Roger Y.  1998.  The Green Fluorescent Protein.  Annual Review in Biochemistry.  67:509-544.&amp;lt;/ref&amp;gt;  The relative amplitudes of these two excitation peaks can vary depending on environmental factors and previous illumination.&amp;lt;ref name=&amp;quot;Ormo&amp;quot; /&amp;gt;  For example, continued excitation leads to a diminution of the 395 nm excitation peak with a reciprocal amplification of the 475 nm peak.&amp;lt;ref name=&amp;quot;Phillips&amp;quot; /&amp;gt;  Regardless of absorption, the chromophore of GFP emits light of 508 nm.&amp;lt;ref name=&amp;quot;Yang&amp;quot; /&amp;gt;&amp;lt;ref name=&amp;quot;Cubitt&amp;quot; /&amp;gt;&amp;lt;ref name=&amp;quot;Ormo&amp;quot; /&amp;gt;&amp;lt;ref name=&amp;quot;Phillips&amp;quot; /&amp;gt;  &lt;br /&gt;
&lt;br /&gt;
Three amino residues in the central α-helix constitute the fluorophore of GFP: Ser&amp;lt;sup&amp;gt;65&amp;lt;/sup&amp;gt;Tyr&amp;lt;sup&amp;gt;66&amp;lt;/sup&amp;gt;Gly&amp;lt;sup&amp;gt;67&amp;lt;/sup&amp;gt; (see below).  Tsien et al. discovered that this tri-peptide sequence is post-translationally modified by internal cyclization and oxidation&amp;lt;ref name=&amp;quot;Haldar&amp;quot; /&amp;gt; to produce a &amp;lt;scene name=&#039;Green_Fluorescent_Protein/Chromophore_structure/1&#039;&amp;gt;4-(p-hydroxybenzylidene)-imidazolidin-5-one&amp;lt;/scene&amp;gt; structure.&amp;lt;ref name=&amp;quot;Yang&amp;quot; /&amp;gt;  Studies with E. coli proposed a sequential mechanism for the formation of the fluorophore that was initiated by a rapid cyclization between Ser&amp;lt;sup&amp;gt;65&amp;lt;/sup&amp;gt; and Gly&amp;lt;sup&amp;gt;67&amp;lt;/sup&amp;gt; to form an imidazolin-5-one intermediate.&amp;lt;ref name=&amp;quot;Yang&amp;quot; /&amp;gt;  This rapid cyclization is carried out via nucleophilic attack of the amino group from Gly&amp;lt;sup&amp;gt;67&amp;lt;/sup&amp;gt; on the carbonyl group of Ser&amp;lt;sup&amp;gt;65&amp;lt;/sup&amp;gt; to form a five-membered ring.  The loss of water then forms the imidazolin-5-one intermediate.&amp;lt;ref name=&amp;quot;Cubitt&amp;quot; /&amp;gt;  Cyclization is succeeded by a much slower rate-limiting oxygenation of the Tyr&amp;lt;sup&amp;gt;66&amp;lt;/sup&amp;gt; hydroxybenzyl side chain by atmospheric oxygen (No fluorescence was seen in anaerobically grown E. coli.), resulting in the 4-(p-hydroxybenzylidene)-imidazolidin-5-one stucture.&amp;lt;ref name=&amp;quot;Yang&amp;quot; /&amp;gt;&amp;lt;ref name=&amp;quot;Cubitt&amp;quot; /&amp;gt;&amp;lt;ref name=&amp;quot;Phillips&amp;quot; /&amp;gt;  The double bond that results from this series of reactions results in the linkage of the two π-systems of the rings, forming a larger conjugated system essential for fluorophore stability. &amp;lt;ref name=&amp;quot;Bublitz&amp;quot;&amp;gt; Bublitz G, King BA, Boxer SG.  1998.  Electronic structure of the chromophore in green fluorescent protein (GFP).  Journal of the American Chemical Society.  120(36): 9370-9371.  DOI 10.1021/ja98160e.&amp;lt;/ref&amp;gt;&lt;br /&gt;
[[Image:GFP Chromophore.png|center|489x360px]]&lt;br /&gt;
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The process is completely auto-catalytic such that there are no known co-factors or enzymatic components required.&amp;lt;ref name=&amp;quot;Yang&amp;quot; /&amp;gt;  Despite the stability of the final product, while the chromophore is forming, the environmental temperature cannot drop below 30°C or the yield of viable GFP will decrease substantially.&amp;lt;ref name=&amp;quot;Yang&amp;quot; /&amp;gt;&amp;lt;ref name=&amp;quot;Phillips&amp;quot; /&amp;gt;  This, of course, is not an issue for the protein in nature as the jellyfish is unlikely to encounter waters of this degree in the Pacific Northwest.&amp;lt;ref name=&amp;quot;Tsien&amp;quot; /&amp;gt;  Such a temperature sensitivity is only relevant during formation as the stability of the final product is maintained through a network of close contacts surrounding the fluorophore.&amp;lt;ref name=&amp;quot;Yang&amp;quot; /&amp;gt;  This, however, can and has been used in [[pulse-chase experiments]] in which the GFP-expressing cells are exposed to varying temperatures in place of labeled vs. unlabeled trials.&amp;lt;ref name=&amp;quot;Tsien&amp;quot; /&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;applet load=&#039;1ema&#039; size=&#039;500&#039; frame=&#039;true&#039; align=&#039;right&#039; scene=&#039;Green_Fluorescent_Protein/Polar_interactions/2&#039; name=&#039;2&#039;/&amp;gt;&lt;br /&gt;
&lt;br /&gt;
As the central α-helix is not located directly in the center of the β-barrel, cavities of differing area exist on either side of the chromophore.  The larger cavity, consisting of about 135 Å,&amp;lt;ref name=&amp;quot;Ormo&amp;quot; /&amp;gt; does not open out to the bulk solvent, but rather houses &amp;lt;scene name=&#039;Green_Fluorescent_Protein/Water_molecules/1&#039;&amp;gt;four water molecules&amp;lt;/scene&amp;gt;.&amp;lt;ref name=&amp;quot;Ormo&amp;quot; /&amp;gt;&amp;lt;ref name=&amp;quot;Van&amp;quot;&amp;gt;van Thor JJ, Sage, JT.  2006.  Charge transfer in green fluorescent protein.  Photochemical &amp;amp; Photobiological Sciences.  5:597-602.  DOI 10.1039/b516525c.&amp;lt;/ref&amp;gt;  Had this space not been occupied, it would be expected to considerably destabilize the protein as a whole.  The hydrogen bonding created by the presence of the water molecules, however, helps to link the buried &amp;lt;scene name=&#039;Green_Fluorescent_Protein/Gln69_glu222/1&#039; target=&#039;2&#039;&amp;gt;side chains&amp;lt;/scene&amp;gt; of Glu&amp;lt;sup&amp;gt;222&amp;lt;/sup&amp;gt; and Gln&amp;lt;sup&amp;gt;69&amp;lt;/sup&amp;gt; that would otherwise be actively polar.&amp;lt;ref name=&amp;quot;Ormo&amp;quot; /&amp;gt;  Therefore, the water molecules are extremely important in establishing a hydrogen bonding network about the chromophor.&amp;lt;ref name=&amp;quot;Lammich&amp;quot;&amp;gt;PMID: 17040991&amp;lt;/ref&amp;gt;&lt;br /&gt;
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The opposite side of the chromophore, however, is within close proximity of several aromatic and polar side chains.  Several &amp;lt;scene name=&#039;Green_Fluorescent_Protein/Polar_interactions/2&#039;&amp;gt;polar interactions&amp;lt;/scene&amp;gt; between the surrounding residues and the chromophore are present including: hydrogen bonds of His&amp;lt;sup&amp;gt;148&amp;lt;/sup&amp;gt;, Thr&amp;lt;sup&amp;gt;203&amp;lt;/sup&amp;gt;, and Ser&amp;lt;sup&amp;gt;205&amp;lt;/sup&amp;gt; with the phenolic hydroxyl of Tyr&amp;lt;sup&amp;gt;66&amp;lt;/sup&amp;gt;; Arg&amp;lt;sup&amp;gt;96&amp;lt;/sup&amp;gt; and Gln&amp;lt;sup&amp;gt;94&amp;lt;/sup&amp;gt; with the carbonyl of the imidazolidinone ring; and hydrogen bonds of Glu&amp;lt;sup&amp;gt;222&amp;lt;/sup&amp;gt; with the side chain of Thr&amp;lt;sup&amp;gt;65&amp;lt;/sup&amp;gt;.  Additional hydrogen bonding in the area around the chromophore helps to stabilize Arg&amp;lt;sup&amp;gt;96&amp;lt;/sup&amp;gt; in the protonated form, which suggests the presence of a partial negative charge on the carbonyl oxygen of the imidazolidinone ring in the deprotonated fluorophore.&amp;lt;ref name=&amp;quot;Ormo&amp;quot; /&amp;gt;  Arg&amp;lt;sup&amp;gt;96&amp;lt;/sup&amp;gt; and Gln&amp;lt;sup&amp;gt;94&amp;lt;/sup&amp;gt; in turn help to steady the imidazolidone.&amp;lt;ref name=&amp;quot;Yang&amp;quot; /&amp;gt;  Therefore, it is thought that Arg&amp;lt;sup&amp;gt;96&amp;lt;/sup&amp;gt; is essential for the formation of the fluorophore by catalyzing the initial ring closure.&amp;lt;ref name=&amp;quot;Ormo&amp;quot; /&amp;gt;  Tyr&amp;lt;sup&amp;gt;145&amp;lt;/sup&amp;gt; provides a stabilizing &lt;br /&gt;
&amp;lt;scene name=&#039;Green_Fluorescent_Protein/Edge_face_interaction/1&#039;&amp;gt;edge-face interaction&amp;lt;/scene&amp;gt;&amp;lt;ref&amp;gt; [http://www.tim.hi-ho.ne.jp/dionisio/ Information about edge-face (CH/π) interactions].&amp;lt;/ref&amp;gt; with the benzyl ring of the chromophore.&amp;lt;ref name=&amp;quot;Ormo&amp;quot; /&amp;gt;  The stability provided by the internal polar interactions are further augmented by the surrounding β-barrel.  &lt;br /&gt;
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The β-barrel provides a highly constrained environment that protects the chromophore from the bulk solvent,&amp;lt;ref name=&amp;quot;Haldar&amp;quot; /&amp;gt; nearly creating the atmosphere of a vacuum.&amp;lt;ref name=&amp;quot;Lammich&amp;quot; /&amp;gt;  This is most likely responsible for the small [[Stoke’s shift]], or the small wavelength difference between excitation and emission.&amp;lt;ref name=&amp;quot;Ormo&amp;quot; /&amp;gt;  &lt;br /&gt;
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{{Link Toggle FancyCartoonHighQualityView}}.&lt;br /&gt;
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Findings show that fluorescence will not occur from a naked chromophore, but rather requires the protection of the β-can structure.&amp;lt;ref name=&amp;quot;Cubitt&amp;quot; /&amp;gt;  However, &#039;&#039;in crystallum&#039;&#039; GFP will exhibit a nearly identical fluorescence spectrum and lifetime when compared with aqueous GFP.  These two elements point to a fluorescence that is not inherent to the isolated fluorophore,&amp;lt;ref name=&amp;quot;Yang&amp;quot; /&amp;gt;&amp;lt;ref name=&amp;quot;Phillips&amp;quot; /&amp;gt; but rather from the auto-catalytic cyclization of the polypeptide sequence Ser&amp;lt;sup&amp;gt;65&amp;lt;/sup&amp;gt;Tyr&amp;lt;sup&amp;gt;66&amp;lt;/sup&amp;gt;Gly&amp;lt;sup&amp;gt;67&amp;lt;/sup&amp;gt; and subsequent oxidation of Tyr&amp;lt;sup&amp;gt;66&amp;lt;/sup&amp;gt;.&amp;lt;ref name=&amp;quot;Phillips&amp;quot; /&amp;gt;  However, this sequence is found in many proteins - why does GFP fluoresce?  According to Phillips (1997), fluorophore formation is due to the close proximity of the backbone atoms between Ser&amp;lt;sup&amp;gt;65&amp;lt;/sup&amp;gt;. and Gly&amp;lt;sup&amp;gt;67&amp;lt;/sup&amp;gt; gained through a lack of sterical hindrance by the hydrogen atom side chain of glycine.  In fact, no functional fluorescent proteins have been found in which any other amino acid other than glycine was found at position 67.  Even so, there are still proteins that have this specific sequence, therefore, there must be another inherent property to GFP that is still left misunderstood.&amp;lt;ref name=&amp;quot;Phillips&amp;quot; /&amp;gt;  &lt;br /&gt;
&lt;br /&gt;
This quandary led Phillips to study the acid/base chemistry catalyzing the initial cyclization of the chromophore.  He found that Arg&amp;lt;sup&amp;gt;96&amp;lt;/sup&amp;gt; actually acts as a &lt;br /&gt;
&amp;lt;scene name=&#039;Green_Fluorescent_Protein/Arg96/1&#039; target=&#039;2&#039; &amp;gt;base&amp;lt;/scene&amp;gt; by withdrawing electrons through hydrogen bonding with the carbonyl oxygen of Ser&amp;lt;sup&amp;gt;65&amp;lt;/sup&amp;gt; to activate the carbonyl carbon for nucleophilic attack by the amide nitrogen of Gly&amp;lt;sup&amp;gt;67&amp;lt;/sup&amp;gt;.  This mechanism was further supported by &#039;&#039;ab initio&#039;&#039; calculations, as well as database searches of similar compounds and protein sequences.  Through acid/base chemistry, the chromophore is stabilized by resonance.&amp;lt;ref name=&amp;quot;Phillips&amp;quot; /&amp;gt;  Femtosecond Raman spectroscopy has been used to map the alteration of the structure close the chromophore during excited-state protein transfer and shown that chromophore wagging is orchestrated by the protein environment.&amp;lt;ref name=&amp;quot;Fang&amp;quot;&amp;gt;PMID: 19907490&amp;lt;/ref&amp;gt;&lt;br /&gt;
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===Mutant Studies===&lt;br /&gt;
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&amp;lt;applet load=&#039;1ema&#039; size=&#039;400&#039; frame=&#039;true&#039; align=&#039;right&#039; scene=&#039;Green_Fluorescent_Protein/1ema_gfp_barrel/2&#039; name=&#039;A&#039;/&amp;gt;&lt;br /&gt;
Many mutant green fluorescent proteins have been developed in order to further understand the structure and mechanism of the fluorophore.  The first mutagenesis studies simply &lt;br /&gt;
&amp;lt;scene name=&#039;Green_Fluorescent_Protein/Truncated_ends/2&#039; target=&#039;A&#039;&amp;gt;truncated the ends&amp;lt;/scene&amp;gt; of the amino acid sequence (&amp;lt;scene name=&#039;Green_Fluorescent_Protein/1ema_gfp_barrel/2&#039; target=&#039;A&#039;&amp;gt;see without truncated ends&amp;lt;/scene&amp;gt;.  NOTE: The structure represented here is already truncated at the carbonyl terminus).  Shortening the polypeptide by more than seven amino acids from either terminus lead to a total loss of fluorescence, as well as a complete failure to absorb light at the traditional wavelengths.   This is most likely due to the structure of the protein.  The last seven amino acid residues of the carboxyl terminus are roughly disordered, and thus do not interfere with the overall structure.  After seven residues, however, the capping α-helix structure is disrupted, leading to an unstable or unformed chromophore.  The &amp;lt;scene name=&#039;Green_Fluorescent_Protein/Amino_terminus/2&#039; target=&#039;A&#039;&amp;gt;amino terminus&amp;lt;/scene&amp;gt; is less understood, but the same principle still applies even though the β-barrel does not begin until residue ten or eleven.&amp;lt;ref name=&amp;quot;Yang&amp;quot; /&amp;gt;  &lt;br /&gt;
&lt;br /&gt;
Point mutations have also been extensively studied in order to examine their effects on the chromophore.  In general, most point mutations lead to a diminished excitation, especially in regions of the sequence adjacent to the fluorophore or those that interact with the fluorophore.  An exception to this trend is the Ser&amp;lt;sup&amp;gt;65&amp;lt;/sup&amp;gt;Thr&amp;lt;sup&amp;gt;66&amp;lt;/sup&amp;gt; mutant (normal Ser&amp;lt;sup&amp;gt;65&amp;lt;/sup&amp;gt;Tyr&amp;lt;sup&amp;gt;66&amp;lt;/sup&amp;gt;), which actually increases fluorescence intensity, although the reason is unclear.&amp;lt;ref name=&amp;quot;Yang&amp;quot; /&amp;gt;&lt;br /&gt;
&lt;br /&gt;
An interesting mutation discovered by Ormo et al. (1996) was the Thr&amp;lt;sup&amp;gt;65&amp;lt;/sup&amp;gt;Tyr&amp;lt;sup&amp;gt;66&amp;lt;/sup&amp;gt;Gly&amp;lt;sup&amp;gt;67&amp;lt;/sup&amp;gt; mutant, which produces an α-helical conformation in the chromophore opposed to the normal conformation, which is nearly perpendicular to the helical axis, due to its interaction with Arg&amp;lt;sup&amp;gt;96&amp;lt;/sup&amp;gt;.  This further supports the idea that Arg&amp;lt;sup&amp;gt;96&amp;lt;/sup&amp;gt; is an important factor in the structural arrangement required for cyclization, perhaps by promoting the attack of Gly&amp;lt;sup&amp;gt;67&amp;lt;/sup&amp;gt; on the carbonyl carbon of Thr&amp;lt;sup&amp;gt;65&amp;lt;/sup&amp;gt;.&amp;lt;ref name=&amp;quot;Ormo&amp;quot; /&amp;gt;&lt;br /&gt;
&lt;br /&gt;
In high protein concentrations, GFP has been found to dimerize under the influence of high ionic strength between the two monomers.  In &#039;&#039;Aequorea victoria&#039;&#039;, the aequorin is able to bind to the &amp;lt;scene name=&#039;Green_Fluorescent_Protein/1gfl/1&#039; target=&#039;A&#039;&amp;gt;dimer&amp;lt;/scene&amp;gt; ([[1gfl]]), but not the monomer.  Therefore, dimerization is a very important structural feature in terms of its function, as it also assists the GFP to absorb energy at the excitation wavelength of aequorin even though GFP has only a “modest” extinction coefficient.  As a result, dimers, and often even higher &amp;lt;scene name=&#039;Green_Fluorescent_Protein/1w7s/1&#039; target=&#039;A&#039;&amp;gt;multimers&amp;lt;/scene&amp;gt; ([[1w7s]]), are predominant protein populations within the jellyfish.&amp;lt;ref name=&amp;quot;Cubitt&amp;quot;&amp;gt;[http://www.sciencedirect.com/science?_ob=ArticleURL&amp;amp;_udi=B6TCV-40W0TN7-50&amp;amp;_user=4187488&amp;amp;_coverDate=11%2F30%2F1995&amp;amp;_rdoc=1&amp;amp;_fmt=high&amp;amp;_orig=search&amp;amp;_sort=d&amp;amp;_docanchor=&amp;amp;view=c&amp;amp;_acct=C000062504&amp;amp;_version=1&amp;amp;_urlVersion=0&amp;amp;_userid=4187488&amp;amp;md5=e92730038bb92b1dfbd4af45a0283cce],Cubitt AB, Heim R, Adams SR, Boyd AE, Gross LA, Tsien R.  1995.  Understanding, improving, and using green fluorescent protein.  Trends in Biochemical Sciences.  20(11): 448-455.  DOI 0.1016/S0968-0004(00)89099-4.&amp;lt;/ref&amp;gt; &lt;br /&gt;
&lt;br /&gt;
{{Link Toggle FancyCartoonHighQualityView}}.&lt;br /&gt;
&lt;br /&gt;
== Using GFP as a Research Tool ==&lt;br /&gt;
&lt;br /&gt;
A description of some of the ways GFP is being used as a tool in research is at [[Green_Fluorscent_Protein:_Research_Tool]].&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
==3D Structures of Green Fluorescent Protein==&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;Update November 2011&#039;&#039;&lt;br /&gt;
&lt;br /&gt;
[[2qu1]], [[2h9w]] – jGFP - jellyfish&amp;lt;br /&amp;gt;&lt;br /&gt;
[[3la1]], [[3i19]], [[2wur]], [[3gex]], [[2qrf]], [[2qt2]], [[2qz0]], [[2gj1]], [[2gj2]], [[3cb9]], [[3cbe]], [[3cd1]], [[3cd9]], [[2hjo]], [[2hqz]], [[2hrs]], [[2okw]], [[2oky]], [[2q57]], [[2due]], [[2duf]], [[2dug]], [[2duh]], [[2dui]], [[2q6p]], [[2hcg]], [[2hfc]], [[2hgd]], [[2hgy]], [[2awj]], [[2awk]], [[2awl]], [[2awm]], [[2g16]], [[2g2s]], [[2g3d]], [[2g5z]], [[2g6e]], [[2ah8]], [[2aha]], [[2fwq]], [[2fzu]], [[2b3p]], [[2b3q]], [[1z1p]], [[1z1q]], [[1yhg]], [[1yhh]], [[1yhi]], [[1yj2]], [[1yjf]], [[1s6z]], [[1q4a]], [[1q4b]], [[1q4c]], [[1q4d]], [[1q4e]], [[1q73]], [[1qyf]], [[1qyo]], [[1qyq]], [[1qst]], [[1qy3]], [[1cv7]], [[1jc0]], [[1jc1]],  [[1jby]], [[1jbz]], [[1kp5]], [[1kyp]], [[1hcj]], [[1h6r]], [[1b9c]], [[1c4f]], [[1emc]], [[1eme]], [[1emf]], [[1emk]], [[1eml]], [[1emm]], [[2emd]], [[2emn]], [[2emo]], [[1emb]], [[1gfl]], [[1ema]], [[2y0g]], [[3gj1]], [[3gj2]], [[3p28]], [[1qxt]] – jGFP (mutant)&amp;lt;br /&amp;gt;&lt;br /&gt;
[[3evp]] – jGFP circular permutation&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2h6v]] – jGFP+imidazole derivative&amp;lt;br /&amp;gt;&lt;br /&gt;
[[1rm9]], [[1rmm]], [[1rmo]], [[1rmp]], [[1rrz]] – jGFP containing fluorotryptophan&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2o24]], [[2o29]], [[2o2b]], [[1w7u]], [[1w7t]], [[1w7s]], [[1emg]] – jGFP (mutant)+imidazole derivative&amp;lt;br /&amp;gt;&lt;br /&gt;
[[1kyr]] – jGFP (mutant)+imidazole derivative+Cu&amp;lt;br /&amp;gt;&lt;br /&gt;
[[1kys]] – jGFP (mutant)+imidazole derivative+Zn&amp;lt;br /&amp;gt;&lt;br /&gt;
[[3ogo]] – jGFP+cGFP nanobody – camel&amp;lt;br /&amp;gt;&lt;br /&gt;
[[3g9a]], [[3k1k]] – jGFP+minimize nanobody – &#039;&#039;Lama pacos&#039;&#039;&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2qle]] – GFP (mutant) – &#039;&#039;Azotobacter vinelandii&#039;&#039;&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2rh7]] – GFP – &#039;&#039;Renilla reniformis&#039;&#039;&amp;lt;br /&amp;gt;&lt;br /&gt;
[[3adf]] – monomeric azami green – &#039;&#039;Galaxea fascicularis&#039;&#039;&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2vzx]] – GFP DENDRA2 – Dendronephthya&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2gw3]] – GFP KAEDE – &#039;&#039;Trachiphyllia geoffroyi&#039;&#039;&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2pox]], [[2gx0]], [[2gx2]], [[2iov]], [[2ie2]] – FP DRONPA – Echinophyllia&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2dd7]] – CpGFP - &#039;&#039;Chiridius poppei&#039;&#039;&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2dd9]] – CpGFP (mutant)&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2c9i]] – saGFP – sea anemone&amp;lt;br /&amp;gt;&lt;br /&gt;
[[1xmz]] – saGFP (mutant)&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2c9j]] – GFP – &#039;&#039;Cerianthus membranaceus&#039;&#039;&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2hpw]] – GFP – &#039;&#039;Clytia gregaria&#039;&#039;&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2g3o]] – PpGFP – &#039;&#039;Pontellina plumata&#039;&#039;&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2g6x]], [[2g6y]] – PpGFP (mutant)&amp;lt;br /&amp;gt;&lt;br /&gt;
[[3lva]], [[3lvc]], [[3lvd]] – GFP (mutant) – &#039;&#039;Aequoarea coerulescens&#039;&#039;&amp;lt;br /&amp;gt;&lt;br /&gt;
&lt;br /&gt;
===Yellow fluorescent protein===&lt;br /&gt;
&lt;br /&gt;
[[3dpw]], [[3dpx]], [[3dpz]], [[3dq1]], [[3dq2]], [[3dq3]], [[3dq4]], [[3dq5]], [[3dq6]], [[3dq7]], [[3dq8]], [[3dq9]], [[3dqa]], [[3dqc]], [[3dqd]], [[3dqe]], [[3dqf]], [[3dqh]], [[3dqi]], [[3dqj]], [[3dqk]], [[3dql]], [[3dqm]], [[3dqn]], [[3dqo]], [[3dqu]], [[1myw]], [[1huy]], [[2yfp]], [[1yfp]] – jGFP (mutant)&amp;lt;br /&amp;gt;&lt;br /&gt;
[[1f09]], [[1f0b]] – jGFP (mutant)+imidazole derivative+I&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2ogr]] – Z-FP - Zoanthus&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2pxs]], [[2pxw]], [[1xa9]], [[1xae]] – Z-FP (mutant)&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2jad]] – jGFP/glutaredoxin&amp;lt;br /&amp;gt;&lt;br /&gt;
&lt;br /&gt;
===Red fluorescent protein===&lt;br /&gt;
&lt;br /&gt;
[[2icr]], [[2ojk]] –  Z-RFP &amp;lt;br /&amp;gt;&lt;br /&gt;
[[2fl1]] – Z-RFP (mutant)&amp;lt;br /&amp;gt;&lt;br /&gt;
[[3bx9]], [[3bxa]], [[3bxb]], [[3bxc]], [[3e5t]], [[3e5w]], [[1uis]], [[3ip2]], [[3pj5]], [[3pj7]], [[3pjb]], [[3pib]] -  EnRFP  – &#039;&#039;Entacmaea quadricolor&#039;&#039;&amp;lt;br /&amp;gt;&lt;br /&gt;
[[3e5v]], [[3rwt]] – EnRFP (mutant)&amp;lt;br /&amp;gt;&lt;br /&gt;
[[1zgo]], [[2vad]], [[2vae]], [[1ggx]] – DiRFP – &#039;&#039;Discosoma&#039;&#039;&amp;lt;br /&amp;gt;&lt;br /&gt;
[[1zgp]], [[1zgq]], [[2h8q]], [[2v4e]], [[1g7k]] – DiRFP (mutant)&amp;lt;br /&amp;gt;&lt;br /&gt;
[[3cfa]] – AsRFP – &#039;&#039;Anemonia sulcata&#039;&#039;&amp;lt;br /&amp;gt;&lt;br /&gt;
[[3nt3]], [[3nt9]] – RFP – artificial gene&amp;lt;br /&amp;gt;&lt;br /&gt;
[[1yzw]] – RFP – &#039;&#039;Heteractis&#039;&#039; &lt;br /&gt;
&lt;br /&gt;
===Cyan fluorescent protein===&lt;br /&gt;
&lt;br /&gt;
[[2wsn]], [[2wso]] - jGFP&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2otb]] – cyan C-FP – Clavularia&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2ote]] - cyan C-FP (mutant)&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2zo6]], [[2zo7]] – cyan FP – &#039;&#039;Fungia concinna&#039;&#039;&amp;lt;br /&amp;gt;&lt;br /&gt;
[[1oxd]], [[1oxe]], [[1oxf]] – cyan FP (mutant) – marker plasmid&amp;lt;br /&amp;gt;&lt;br /&gt;
&lt;br /&gt;
===Blue fluorescent protein===&lt;br /&gt;
&lt;br /&gt;
[[1bfp]] – jGFP (mutant)&lt;br /&gt;
&lt;br /&gt;
===Photoconvertible fluorescent protein===&lt;br /&gt;
&lt;br /&gt;
[[2vvh]], [[2vvi]], [[2vvj]], [[3p8u]] –  LhGFP (mutant) – &#039;&#039;Lobophyllia hemprichii&#039;&#039;&amp;lt;br /&amp;gt;&lt;br /&gt;
[[1zux]] –  LhGFP&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2btj]] -  LhGFP+imidazole derivative&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2ddc]], [[1xss]] –  FfFP – &#039;&#039;Favia favus&#039;&#039;&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2ddd]] -  FfFP (mutant)&amp;lt;br /&amp;gt;&lt;br /&gt;
[[3cff]], [[3cfh]] – AsGFP (mutant)&lt;br /&gt;
&lt;br /&gt;
===Green fluorescent protein chimera===&lt;br /&gt;
&lt;br /&gt;
[[3ai4]] – jGFP/mPolymerase iota ubiquitin binding motif - mouse&amp;lt;br /&amp;gt;&lt;br /&gt;
[[3ai5]] - jGFP/m ubiquitin&amp;lt;br /&amp;gt;&lt;br /&gt;
[[3o77]], [[3o78]], [[3ek4]], [[3ek7]] - jGFP/myosin light chain kinase/calmodulin&amp;lt;br /&amp;gt;&lt;br /&gt;
[[3evr]], [[3evu]], [[3evv]] - jGFP/myosin light chain kinase/calmodulin+Ca&amp;lt;br /&amp;gt;&lt;br /&gt;
[[3ek8]], [[3ekh]], [[3ekj]] - jGFP/myosin light chain kinase/calmodulin (mutant)&amp;lt;br /&amp;gt;&lt;br /&gt;
[[3osq]], [[3osr]] – jGFP/maltose-binding protein&lt;br /&gt;
 &lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
==Reference for this Structure==&lt;br /&gt;
&lt;br /&gt;
Ormo M, Cubitt AB, Kallio K, Gross LA, Tsien RY, Remington SJ.  1996.  Crystal structure of the &#039;&#039;Aequorea victoria&#039;&#039; green fluorescent protein.  Science.  273(5280):1392-1395.  [http://www.sciencemag.org/cgi/content/abstract/273/5280/1392 DOI 10.1126/science.273.5280.1392].&lt;br /&gt;
&lt;br /&gt;
==References==&lt;br /&gt;
&lt;br /&gt;
{{Reflist}}&lt;br /&gt;
&lt;br /&gt;
==Additional Resources==&lt;br /&gt;
*For additional information, see: [[Colored &amp;amp; Bioluminescent Proteins]]&lt;br /&gt;
*[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ema First Glance]&lt;br /&gt;
*PDBsum: [http://www.ebi.ac.uk/pdbsum/1ema 1ema]&lt;br /&gt;
*RCSB PDB [http://www.rcsb.org/pdb/explore.do?structureId=1ema 1ema]&lt;br /&gt;
*[http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ema OCA]&lt;br /&gt;
*UniProt: [http://www.uniprot.org/uniprot/P42212 P42212]&lt;br /&gt;
*Scop: [http://scop.mrc-lmb.cam.ac.uk/scop/data/scop.b.e.gc.b.b.b.html P42212]&lt;br /&gt;
*CATH: [http://www.cathdb.info/domain/1emaA00 1emaA00]&lt;br /&gt;
*Pfam: [http://pfam.sanger.ac.uk/family?acc=PF01353 PF01353]&lt;br /&gt;
*InterPro: [http://www.ebi.ac.uk/interpro/ISearch?query=IPR000786 IPR000786]&lt;br /&gt;
*[http://www.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb42_1.html GFP featured] at the &#039;&#039;&#039;[http://www.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month]&#039;&#039;&#039; series of tutorials by [[User:David_S._Goodsell|David Goodsell]].&lt;br /&gt;
* [http://www.nature.com/nature/journal/v462/n7270/edsumm/e091112-05.html Inside green fluorescent protein] - editor&#039;s summary that accompanied [http://www.nature.com/nature/journal/v462/n7270/covers/ structural detail of GFP chromophore on the cover] of Nature.&lt;br /&gt;
&lt;br /&gt;
[[he:GFP_(Hebrew)]]&lt;br /&gt;
&lt;br /&gt;
[[Category:Topic Page]]&lt;/div&gt;</summary>
		<author><name>Jing Liu</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1329562</id>
		<title>User:Jing Liu/Sandbox 1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1329562"/>
		<updated>2011-12-07T17:35:58Z</updated>

		<summary type="html">&lt;p&gt;Jing Liu: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;[[[[Green Fluorescent Protein]]]]&amp;lt;applet load=&#039;1ema&#039; size=&#039;450&#039; frame=&#039;true&#039; align=&#039;right&#039; scene=&#039;Green_Fluorescent_Protein/1ema_gfp_default/2&#039; caption=&#039;Green fluorescent protein complex with peptide-derived chromophore ([[1ema]])&#039; /&amp;gt; &lt;br /&gt;
&#039;&#039;&#039;Green fluorescent protein (GFP)&#039;&#039;&#039; is a [[bioluminescent]] polypeptide consisting of 238 residues isolated from the body of [[Aequorea victoria]] jellyfish.&amp;lt;ref name=&amp;quot;PDBsum&amp;quot;&amp;gt;[http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=1ema&amp;amp;template=main.html], Protein Database (PDBsum): 1ema.  European Bioinformatics (EBI); 2009.&amp;lt;/ref&amp;gt; GFP converts the blue chemiluminescent of [[aequorin]] in the jellyfish into green fluorescent light.&amp;lt;ref name=&amp;quot;Yang&amp;quot;&amp;gt;[http://www-bioc.rice.edu/Bioch/Phillips/Papers/gfpbio.html], Yang F, Moss LG, Phillips GN Jr.  1996.  The molecular structure of green fluorescent protein.  Biotechnology.  14: 1246-1251.  DOI 10.1038/nbt1096-1246.&amp;lt;/ref&amp;gt; It remains unclear why these jellyfish use fluorescence, why green is better than blue, or why they produce a separate protein for green fluorescence as opposed to simply mutating the present aequorin to shift its wavelength,&amp;lt;ref name=&amp;quot;Tsien&amp;quot; /&amp;gt; but in the laboratory, GFP can be incorporated into a variety of biological systems in order to function as a marker protein. Since its discovery in 1962, GFP has become a significant contributor to the research of monitoring gene expression, localization, mobility, traffic, interactions between various membrane and cytoplasmic proteins, as well as many others.&amp;lt;ref name=&amp;quot;Haldar&amp;quot;&amp;gt;[http://www.springerlink.com/content/wvg513864266g77n/fulltext.pdf], Haldar S, Chattopadhyay A.  2009.  The green journey.  J Fluoresc.  19:1-2.  DOI 10.1007/s10895-008-0455-6; biographical background on [http://en.wikipedia.org/wiki/Douglas_Prasher Douglas Prasher], [http://en.wikipedia.org/wiki/Martin_Chalfie Martin Chalfie] and [http://en.wikipedia.org/wiki/Roger_Tsien Roger Tsien].&amp;lt;/ref&amp;gt;&lt;br /&gt;
&lt;br /&gt;
==History==&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;Aequorea victoria&#039;&#039; was first discovered and investigated for its bioluminescence by Frank Johnson, who invited Osamu Shimomura to work with him in on a small island not far from British Columbia, where the jellyfish is abundant.&amp;lt;ref name=&amp;quot;Shimomura&amp;quot;&amp;gt;[http://nobelprize.org/nobel_prizes/chemistry/laureates/2008/shimomura_lecture.pdf], Shimomura O.  The discovery of green fluorescent protein.  Nobel Prize Lecture; 2009;; biographical background at [http://en.wikipedia.org/wiki/Osamu_Shimomura Wikipedia].&amp;lt;/ref&amp;gt; Found off the west coast of the United States between British Columbia and central California,&amp;lt;ref name=&amp;quot;Cowles&amp;quot;&amp;gt;[http://www.wallawalla.edu/academics/departments/biology/rosario/inverts/Cnidaria/Class-Hydrozoa/Hydromedusae/Aequorea_victoria.html],Cowles D, Cowles J.  &#039;&#039;Aequorea victoria&#039;&#039;.  2007.  Walla Wall University.&amp;lt;/ref&amp;gt; the jellyfish was considered a local phenomenon as it would drift in and out of the harbors.&amp;lt;ref name=&amp;quot;Shimomura&amp;quot; /&amp;gt;&lt;br /&gt;
[[Image:GFP mice.png|thumb|left|450x200px|Mice with GFP inserted into their genomes for neurology studies.]]&lt;br /&gt;
&lt;br /&gt;
Shimomura was originally looking only to isolate the blue luminescent protein of &#039;&#039;Aequorea victoria&#039;&#039;, traditionally thought to be [[luciferase]], but it would soon become apparent that the glow was in fact due to aequorin, a substance related, but slightly varying from luciferase.&amp;lt;ref name=&amp;quot;Haldar&amp;quot; /&amp;gt;&amp;lt;ref name=&amp;quot;Shimomura&amp;quot; /&amp;gt; However, the light emitted from aequorin still differed from the light emitted from the wild jellyfish. This quandary led to the discovery of the green fluorescent protein responsible for this disparity, but sufficient amounts of the protein could not be collected for study until 1979. The journey to discover the nature of GFP had begun.&amp;lt;ref name=&amp;quot;Shimomura&amp;quot; /&amp;gt;&lt;br /&gt;
&lt;br /&gt;
In the 1990’s, Douglas Prasher, Frank Predergast, and co-workers successfully cloned the gene that encoded for GFP.  Martin Chalfie further pursued this line of work and was eventually able to express GFP in heterologous systems such as E. coli and C. elegans.  Chalfie’s research provided the first evidence that GFP was unique as it did not require the presence of any exogenous substance or cofactor for fluorescence.&amp;lt;ref name=&amp;quot;Haldar&amp;quot; /&amp;gt; The lack for the need for a cofactor proved that the cloned GFP gene contained all the information necessary for posttranslational synthesis of the chromophore. &amp;lt;ref name=&amp;quot;Tsien&amp;quot; /&amp;gt;&lt;br /&gt;
&lt;br /&gt;
Roger Tsien and co-workers were intrigued by the absence of a necessary cofactor and began to research the structure of GFP and how it relates to its fluorescence.  They discovered that a helix within the beta barrel structure of GFP actually contained a fluorophore responsible for fluorescence.  In researching its structure, they were able to develop GFP derivatives with improved fluorescence and photo-stability.  Shimomura, Chalfie, and Tsien were each recognized for their work involving GFP with the Nobel Prize in 2008.&amp;lt;ref name=&amp;quot;Haldar&amp;quot; /&amp;gt;  In the time since the work of these three researchers, GFP has been successfully expressed and utilized in bacteria, yeast, slime mold, plants, drosophila fruit flies, zebra-fish, and mammalian cells.&amp;lt;ref name=&amp;quot;Yang&amp;quot; /&amp;gt;  Below, mice have had GFP inserted into their genomes for studies in neurology.&lt;br /&gt;
&lt;br /&gt;
==Structure==&lt;br /&gt;
&lt;br /&gt;
===Primary &amp;amp; Secondary Structure===&lt;br /&gt;
{{STRUCTURE_1ema |  SIZE=400 |PDB=1ema  |  SCENE=Green_Fluorescent_Protein/1ema_gfp_default/2 |CAPTION = 1ema, resolution 1.90&amp;amp;Aring; (&amp;lt;scene name=&#039;Green_Fluorescent_Protein/1ema_gfp_default/2&#039;&amp;gt;default scene&amp;lt;/scene&amp;gt;).}}&lt;br /&gt;
Green fluorescent protein (&amp;lt;scene name=&#039;Green_Fluorescent_Protein/1ema_gfp_default/2&#039;&amp;gt;default scene&amp;lt;/scene&amp;gt;) is a 21 kDa protein consisting of 238 residues strung together&amp;lt;ref&amp;gt;Primary structure at [http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=1ema&amp;amp;template=protein.html&amp;amp;r=wiring&amp;amp;l=1&amp;amp;chain=A www.ebi.aci.uk].&amp;lt;/ref&amp;gt; to form a  &lt;br /&gt;
&amp;lt;scene name=&#039;Green_Fluorescent_Protein/1ema_gfp_barrel/2&#039;&amp;gt;secondary structure&amp;lt;/scene&amp;gt; of five α-helices and one eleven-stranded β-pleated sheet,&amp;lt;ref name=&amp;quot;PDBsum&amp;quot; /&amp;gt; where each strand contains nine to thirteen residues each.&amp;lt;ref name=&amp;quot;Ormo&amp;quot; /&amp;gt;  (To view the primary and secondary structure of GFP, go to .)  These β-strands display an almost “seamless symmetry” in which only two of the strands vary in structural content.&amp;lt;ref name=&amp;quot;Phillips&amp;quot;&amp;gt;PMID: 9434902&amp;lt;/ref&amp;gt;  This β-sheet conforms itself through regular hydrogen bonding into a β-barrel.&amp;lt;ref name=&amp;quot;Yang&amp;quot; /&amp;gt;  In GFP, the structure is so regular that &amp;lt;scene name=&#039;Green_Fluorescent_Protein/Water_stripes/1&#039;&amp;gt;&amp;quot;stripes&amp;quot;&amp;lt;/scene&amp;gt; of water molecules (red) can be seen following the structure of the barrel.&amp;lt;ref name=&amp;quot;Phillips&amp;quot; /&amp;gt;  Together with the α-helices at either end of the molecule, a nearly perfect cylinder is produced, 42Å long and 24Å in diameter,&amp;lt;ref name=&amp;quot;Ormo&amp;quot; /&amp;gt; creating what is referred to as a “β-can” formation.&amp;lt;ref name=&amp;quot;Phillips&amp;quot; /&amp;gt;  The short helical segments at either end of the cylinder form “caps” to further protect the interior of the β-barrel.&amp;lt;ref name=&amp;quot;Phillips&amp;quot; /&amp;gt;  Overall stability is maintained by this β-can structure, helping to resist unfolding from heat and other denaturants.&amp;lt;ref name=&amp;quot;Yang&amp;quot; /&amp;gt;&lt;br /&gt;
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One &amp;lt;scene name=&#039;Green_Fluorescent_Protein/Central_helix/1&#039;&amp;gt;α-helix&amp;lt;/scene&amp;gt; can be found running through the central axis of the β-barrel,&amp;lt;ref name=&amp;quot;Haldar&amp;quot; /&amp;gt; roughly &amp;lt;scene name=&#039;Green_Fluorescent_Protein/Perpendicular/1&#039;&amp;gt;perpendicular&amp;lt;/scene&amp;gt; to the symmetry axis of the barrel.&amp;lt;ref name=&amp;quot;Ormo&amp;quot;&amp;gt;Ormo M, Cubitt AB, Kallio K, Gross LA, Tsien RY, Remington SJ.  1996.  Crystal structure of the &#039;&#039;Aequorea victoria&#039;&#039; green fluorescent protein.  Science.  273(5280):1392-1395.  DOI 10.1126/science.273.5280.1392.&amp;lt;/ref&amp;gt;  This helix is extremely important as it contains the fluorophore responsible for fluorescence.&amp;lt;ref name=&amp;quot;Yang&amp;quot; /&amp;gt;&amp;lt;ref name=&amp;quot;Haldar&amp;quot; /&amp;gt;  This α-helix in particular is highly stabilized by the many &amp;lt;scene name=&#039;Green_Fluorescent_Protein/Spacefill/1&#039;&amp;gt;contacts&amp;lt;/scene&amp;gt; that are made with each strand of the barrel.&amp;lt;ref name=&amp;quot;Andrews&amp;quot;&amp;gt;PMID:18713871&amp;lt;/ref&amp;gt;&lt;br /&gt;
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{{Link Toggle FancyCartoonHighQualityView}}.&lt;br /&gt;
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===The Chromophore===&lt;br /&gt;
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The &amp;lt;scene name=&#039;Green_Fluorescent_Protein/Chromophore/1&#039;&amp;gt;chromophore&amp;lt;/scene&amp;gt; (&amp;lt;scene name=&#039;Green_Fluorescent_Protein/1ema_gfp_chromophorezoom/6&#039;&amp;gt;top view&amp;lt;/scene&amp;gt;) of GFP is located at the center of the β-barrel with a wild-type excitation peak of 395 nm, and a minor peak at 475 nm (about three times less intense&amp;lt;ref name=&amp;quot;Tsien&amp;quot; /&amp;gt;) &amp;lt;ref name=&amp;quot;Yang&amp;quot; /&amp;gt;&amp;lt;ref name=&amp;quot;Cubitt&amp;quot; /&amp;gt;&amp;lt;ref name=&amp;quot;Ormo&amp;quot; /&amp;gt;&amp;lt;ref name=&amp;quot;Phillips&amp;quot; /&amp;gt; with extinction coefficients of approximately 30,000 and 7,000 M&amp;lt;sup&amp;gt;-1&amp;lt;/sup&amp;gt; cm&amp;lt;sup&amp;gt;-1&amp;lt;/sup&amp;gt;, respectively.&amp;lt;ref name=&amp;quot;Yang&amp;quot; /&amp;gt;&amp;lt;ref name=&amp;quot;Phillips&amp;quot; /&amp;gt;  Interestingly, the &#039;&#039;Aequorea victoria&#039;&#039; jellyfish utilizes the smaller of the two excitation peaks as pure aequorin emits a light of 470 nm.&amp;lt;ref name=&amp;quot;Tsien&amp;quot;&amp;gt;Tsien, Roger Y.  1998.  The Green Fluorescent Protein.  Annual Review in Biochemistry.  67:509-544.&amp;lt;/ref&amp;gt;  The relative amplitudes of these two excitation peaks can vary depending on environmental factors and previous illumination.&amp;lt;ref name=&amp;quot;Ormo&amp;quot; /&amp;gt;  For example, continued excitation leads to a diminution of the 395 nm excitation peak with a reciprocal amplification of the 475 nm peak.&amp;lt;ref name=&amp;quot;Phillips&amp;quot; /&amp;gt;  Regardless of absorption, the chromophore of GFP emits light of 508 nm.&amp;lt;ref name=&amp;quot;Yang&amp;quot; /&amp;gt;&amp;lt;ref name=&amp;quot;Cubitt&amp;quot; /&amp;gt;&amp;lt;ref name=&amp;quot;Ormo&amp;quot; /&amp;gt;&amp;lt;ref name=&amp;quot;Phillips&amp;quot; /&amp;gt;  &lt;br /&gt;
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Three amino residues in the central α-helix constitute the fluorophore of GFP: Ser&amp;lt;sup&amp;gt;65&amp;lt;/sup&amp;gt;Tyr&amp;lt;sup&amp;gt;66&amp;lt;/sup&amp;gt;Gly&amp;lt;sup&amp;gt;67&amp;lt;/sup&amp;gt; (see below).  Tsien et al. discovered that this tri-peptide sequence is post-translationally modified by internal cyclization and oxidation&amp;lt;ref name=&amp;quot;Haldar&amp;quot; /&amp;gt; to produce a &amp;lt;scene name=&#039;Green_Fluorescent_Protein/Chromophore_structure/1&#039;&amp;gt;4-(p-hydroxybenzylidene)-imidazolidin-5-one&amp;lt;/scene&amp;gt; structure.&amp;lt;ref name=&amp;quot;Yang&amp;quot; /&amp;gt;  Studies with E. coli proposed a sequential mechanism for the formation of the fluorophore that was initiated by a rapid cyclization between Ser&amp;lt;sup&amp;gt;65&amp;lt;/sup&amp;gt; and Gly&amp;lt;sup&amp;gt;67&amp;lt;/sup&amp;gt; to form an imidazolin-5-one intermediate.&amp;lt;ref name=&amp;quot;Yang&amp;quot; /&amp;gt;  This rapid cyclization is carried out via nucleophilic attack of the amino group from Gly&amp;lt;sup&amp;gt;67&amp;lt;/sup&amp;gt; on the carbonyl group of Ser&amp;lt;sup&amp;gt;65&amp;lt;/sup&amp;gt; to form a five-membered ring.  The loss of water then forms the imidazolin-5-one intermediate.&amp;lt;ref name=&amp;quot;Cubitt&amp;quot; /&amp;gt;  Cyclization is succeeded by a much slower rate-limiting oxygenation of the Tyr&amp;lt;sup&amp;gt;66&amp;lt;/sup&amp;gt; hydroxybenzyl side chain by atmospheric oxygen (No fluorescence was seen in anaerobically grown E. coli.), resulting in the 4-(p-hydroxybenzylidene)-imidazolidin-5-one stucture.&amp;lt;ref name=&amp;quot;Yang&amp;quot; /&amp;gt;&amp;lt;ref name=&amp;quot;Cubitt&amp;quot; /&amp;gt;&amp;lt;ref name=&amp;quot;Phillips&amp;quot; /&amp;gt;  The double bond that results from this series of reactions results in the linkage of the two π-systems of the rings, forming a larger conjugated system essential for fluorophore stability. &amp;lt;ref name=&amp;quot;Bublitz&amp;quot;&amp;gt; Bublitz G, King BA, Boxer SG.  1998.  Electronic structure of the chromophore in green fluorescent protein (GFP).  Journal of the American Chemical Society.  120(36): 9370-9371.  DOI 10.1021/ja98160e.&amp;lt;/ref&amp;gt;&lt;br /&gt;
[[Image:GFP Chromophore.png|center|489x360px]]&lt;br /&gt;
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The process is completely auto-catalytic such that there are no known co-factors or enzymatic components required.&amp;lt;ref name=&amp;quot;Yang&amp;quot; /&amp;gt;  Despite the stability of the final product, while the chromophore is forming, the environmental temperature cannot drop below 30°C or the yield of viable GFP will decrease substantially.&amp;lt;ref name=&amp;quot;Yang&amp;quot; /&amp;gt;&amp;lt;ref name=&amp;quot;Phillips&amp;quot; /&amp;gt;  This, of course, is not an issue for the protein in nature as the jellyfish is unlikely to encounter waters of this degree in the Pacific Northwest.&amp;lt;ref name=&amp;quot;Tsien&amp;quot; /&amp;gt;  Such a temperature sensitivity is only relevant during formation as the stability of the final product is maintained through a network of close contacts surrounding the fluorophore.&amp;lt;ref name=&amp;quot;Yang&amp;quot; /&amp;gt;  This, however, can and has been used in [[pulse-chase experiments]] in which the GFP-expressing cells are exposed to varying temperatures in place of labeled vs. unlabeled trials.&amp;lt;ref name=&amp;quot;Tsien&amp;quot; /&amp;gt;&lt;br /&gt;
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&amp;lt;applet load=&#039;1ema&#039; size=&#039;500&#039; frame=&#039;true&#039; align=&#039;right&#039; scene=&#039;Green_Fluorescent_Protein/Polar_interactions/2&#039; name=&#039;2&#039;/&amp;gt;&lt;br /&gt;
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As the central α-helix is not located directly in the center of the β-barrel, cavities of differing area exist on either side of the chromophore.  The larger cavity, consisting of about 135 Å,&amp;lt;ref name=&amp;quot;Ormo&amp;quot; /&amp;gt; does not open out to the bulk solvent, but rather houses &amp;lt;scene name=&#039;Green_Fluorescent_Protein/Water_molecules/1&#039;&amp;gt;four water molecules&amp;lt;/scene&amp;gt;.&amp;lt;ref name=&amp;quot;Ormo&amp;quot; /&amp;gt;&amp;lt;ref name=&amp;quot;Van&amp;quot;&amp;gt;van Thor JJ, Sage, JT.  2006.  Charge transfer in green fluorescent protein.  Photochemical &amp;amp; Photobiological Sciences.  5:597-602.  DOI 10.1039/b516525c.&amp;lt;/ref&amp;gt;  Had this space not been occupied, it would be expected to considerably destabilize the protein as a whole.  The hydrogen bonding created by the presence of the water molecules, however, helps to link the buried &amp;lt;scene name=&#039;Green_Fluorescent_Protein/Gln69_glu222/1&#039; target=&#039;2&#039;&amp;gt;side chains&amp;lt;/scene&amp;gt; of Glu&amp;lt;sup&amp;gt;222&amp;lt;/sup&amp;gt; and Gln&amp;lt;sup&amp;gt;69&amp;lt;/sup&amp;gt; that would otherwise be actively polar.&amp;lt;ref name=&amp;quot;Ormo&amp;quot; /&amp;gt;  Therefore, the water molecules are extremely important in establishing a hydrogen bonding network about the chromophor.&amp;lt;ref name=&amp;quot;Lammich&amp;quot;&amp;gt;PMID: 17040991&amp;lt;/ref&amp;gt;&lt;br /&gt;
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The opposite side of the chromophore, however, is within close proximity of several aromatic and polar side chains.  Several &amp;lt;scene name=&#039;Green_Fluorescent_Protein/Polar_interactions/2&#039;&amp;gt;polar interactions&amp;lt;/scene&amp;gt; between the surrounding residues and the chromophore are present including: hydrogen bonds of His&amp;lt;sup&amp;gt;148&amp;lt;/sup&amp;gt;, Thr&amp;lt;sup&amp;gt;203&amp;lt;/sup&amp;gt;, and Ser&amp;lt;sup&amp;gt;205&amp;lt;/sup&amp;gt; with the phenolic hydroxyl of Tyr&amp;lt;sup&amp;gt;66&amp;lt;/sup&amp;gt;; Arg&amp;lt;sup&amp;gt;96&amp;lt;/sup&amp;gt; and Gln&amp;lt;sup&amp;gt;94&amp;lt;/sup&amp;gt; with the carbonyl of the imidazolidinone ring; and hydrogen bonds of Glu&amp;lt;sup&amp;gt;222&amp;lt;/sup&amp;gt; with the side chain of Thr&amp;lt;sup&amp;gt;65&amp;lt;/sup&amp;gt;.  Additional hydrogen bonding in the area around the chromophore helps to stabilize Arg&amp;lt;sup&amp;gt;96&amp;lt;/sup&amp;gt; in the protonated form, which suggests the presence of a partial negative charge on the carbonyl oxygen of the imidazolidinone ring in the deprotonated fluorophore.&amp;lt;ref name=&amp;quot;Ormo&amp;quot; /&amp;gt;  Arg&amp;lt;sup&amp;gt;96&amp;lt;/sup&amp;gt; and Gln&amp;lt;sup&amp;gt;94&amp;lt;/sup&amp;gt; in turn help to steady the imidazolidone.&amp;lt;ref name=&amp;quot;Yang&amp;quot; /&amp;gt;  Therefore, it is thought that Arg&amp;lt;sup&amp;gt;96&amp;lt;/sup&amp;gt; is essential for the formation of the fluorophore by catalyzing the initial ring closure.&amp;lt;ref name=&amp;quot;Ormo&amp;quot; /&amp;gt;  Tyr&amp;lt;sup&amp;gt;145&amp;lt;/sup&amp;gt; provides a stabilizing &lt;br /&gt;
&amp;lt;scene name=&#039;Green_Fluorescent_Protein/Edge_face_interaction/1&#039;&amp;gt;edge-face interaction&amp;lt;/scene&amp;gt;&amp;lt;ref&amp;gt; [http://www.tim.hi-ho.ne.jp/dionisio/ Information about edge-face (CH/π) interactions].&amp;lt;/ref&amp;gt; with the benzyl ring of the chromophore.&amp;lt;ref name=&amp;quot;Ormo&amp;quot; /&amp;gt;  The stability provided by the internal polar interactions are further augmented by the surrounding β-barrel.  &lt;br /&gt;
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The β-barrel provides a highly constrained environment that protects the chromophore from the bulk solvent,&amp;lt;ref name=&amp;quot;Haldar&amp;quot; /&amp;gt; nearly creating the atmosphere of a vacuum.&amp;lt;ref name=&amp;quot;Lammich&amp;quot; /&amp;gt;  This is most likely responsible for the small [[Stoke’s shift]], or the small wavelength difference between excitation and emission.&amp;lt;ref name=&amp;quot;Ormo&amp;quot; /&amp;gt;  &lt;br /&gt;
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{{Link Toggle FancyCartoonHighQualityView}}.&lt;br /&gt;
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Findings show that fluorescence will not occur from a naked chromophore, but rather requires the protection of the β-can structure.&amp;lt;ref name=&amp;quot;Cubitt&amp;quot; /&amp;gt;  However, &#039;&#039;in crystallum&#039;&#039; GFP will exhibit a nearly identical fluorescence spectrum and lifetime when compared with aqueous GFP.  These two elements point to a fluorescence that is not inherent to the isolated fluorophore,&amp;lt;ref name=&amp;quot;Yang&amp;quot; /&amp;gt;&amp;lt;ref name=&amp;quot;Phillips&amp;quot; /&amp;gt; but rather from the auto-catalytic cyclization of the polypeptide sequence Ser&amp;lt;sup&amp;gt;65&amp;lt;/sup&amp;gt;Tyr&amp;lt;sup&amp;gt;66&amp;lt;/sup&amp;gt;Gly&amp;lt;sup&amp;gt;67&amp;lt;/sup&amp;gt; and subsequent oxidation of Tyr&amp;lt;sup&amp;gt;66&amp;lt;/sup&amp;gt;.&amp;lt;ref name=&amp;quot;Phillips&amp;quot; /&amp;gt;  However, this sequence is found in many proteins - why does GFP fluoresce?  According to Phillips (1997), fluorophore formation is due to the close proximity of the backbone atoms between Ser&amp;lt;sup&amp;gt;65&amp;lt;/sup&amp;gt;. and Gly&amp;lt;sup&amp;gt;67&amp;lt;/sup&amp;gt; gained through a lack of sterical hindrance by the hydrogen atom side chain of glycine.  In fact, no functional fluorescent proteins have been found in which any other amino acid other than glycine was found at position 67.  Even so, there are still proteins that have this specific sequence, therefore, there must be another inherent property to GFP that is still left misunderstood.&amp;lt;ref name=&amp;quot;Phillips&amp;quot; /&amp;gt;  &lt;br /&gt;
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This quandary led Phillips to study the acid/base chemistry catalyzing the initial cyclization of the chromophore.  He found that Arg&amp;lt;sup&amp;gt;96&amp;lt;/sup&amp;gt; actually acts as a &lt;br /&gt;
&amp;lt;scene name=&#039;Green_Fluorescent_Protein/Arg96/1&#039; target=&#039;2&#039; &amp;gt;base&amp;lt;/scene&amp;gt; by withdrawing electrons through hydrogen bonding with the carbonyl oxygen of Ser&amp;lt;sup&amp;gt;65&amp;lt;/sup&amp;gt; to activate the carbonyl carbon for nucleophilic attack by the amide nitrogen of Gly&amp;lt;sup&amp;gt;67&amp;lt;/sup&amp;gt;.  This mechanism was further supported by &#039;&#039;ab initio&#039;&#039; calculations, as well as database searches of similar compounds and protein sequences.  Through acid/base chemistry, the chromophore is stabilized by resonance.&amp;lt;ref name=&amp;quot;Phillips&amp;quot; /&amp;gt;  Femtosecond Raman spectroscopy has been used to map the alteration of the structure close the chromophore during excited-state protein transfer and shown that chromophore wagging is orchestrated by the protein environment.&amp;lt;ref name=&amp;quot;Fang&amp;quot;&amp;gt;PMID: 19907490&amp;lt;/ref&amp;gt;&lt;br /&gt;
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===Mutant Studies===&lt;br /&gt;
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&amp;lt;applet load=&#039;1ema&#039; size=&#039;400&#039; frame=&#039;true&#039; align=&#039;right&#039; scene=&#039;Green_Fluorescent_Protein/1ema_gfp_barrel/2&#039; name=&#039;A&#039;/&amp;gt;&lt;br /&gt;
Many mutant green fluorescent proteins have been developed in order to further understand the structure and mechanism of the fluorophore.  The first mutagenesis studies simply &lt;br /&gt;
&amp;lt;scene name=&#039;Green_Fluorescent_Protein/Truncated_ends/2&#039; target=&#039;A&#039;&amp;gt;truncated the ends&amp;lt;/scene&amp;gt; of the amino acid sequence (&amp;lt;scene name=&#039;Green_Fluorescent_Protein/1ema_gfp_barrel/2&#039; target=&#039;A&#039;&amp;gt;see without truncated ends&amp;lt;/scene&amp;gt;.  NOTE: The structure represented here is already truncated at the carbonyl terminus).  Shortening the polypeptide by more than seven amino acids from either terminus lead to a total loss of fluorescence, as well as a complete failure to absorb light at the traditional wavelengths.   This is most likely due to the structure of the protein.  The last seven amino acid residues of the carboxyl terminus are roughly disordered, and thus do not interfere with the overall structure.  After seven residues, however, the capping α-helix structure is disrupted, leading to an unstable or unformed chromophore.  The &amp;lt;scene name=&#039;Green_Fluorescent_Protein/Amino_terminus/2&#039; target=&#039;A&#039;&amp;gt;amino terminus&amp;lt;/scene&amp;gt; is less understood, but the same principle still applies even though the β-barrel does not begin until residue ten or eleven.&amp;lt;ref name=&amp;quot;Yang&amp;quot; /&amp;gt;  &lt;br /&gt;
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Point mutations have also been extensively studied in order to examine their effects on the chromophore.  In general, most point mutations lead to a diminished excitation, especially in regions of the sequence adjacent to the fluorophore or those that interact with the fluorophore.  An exception to this trend is the Ser&amp;lt;sup&amp;gt;65&amp;lt;/sup&amp;gt;Thr&amp;lt;sup&amp;gt;66&amp;lt;/sup&amp;gt; mutant (normal Ser&amp;lt;sup&amp;gt;65&amp;lt;/sup&amp;gt;Tyr&amp;lt;sup&amp;gt;66&amp;lt;/sup&amp;gt;), which actually increases fluorescence intensity, although the reason is unclear.&amp;lt;ref name=&amp;quot;Yang&amp;quot; /&amp;gt;&lt;br /&gt;
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An interesting mutation discovered by Ormo et al. (1996) was the Thr&amp;lt;sup&amp;gt;65&amp;lt;/sup&amp;gt;Tyr&amp;lt;sup&amp;gt;66&amp;lt;/sup&amp;gt;Gly&amp;lt;sup&amp;gt;67&amp;lt;/sup&amp;gt; mutant, which produces an α-helical conformation in the chromophore opposed to the normal conformation, which is nearly perpendicular to the helical axis, due to its interaction with Arg&amp;lt;sup&amp;gt;96&amp;lt;/sup&amp;gt;.  This further supports the idea that Arg&amp;lt;sup&amp;gt;96&amp;lt;/sup&amp;gt; is an important factor in the structural arrangement required for cyclization, perhaps by promoting the attack of Gly&amp;lt;sup&amp;gt;67&amp;lt;/sup&amp;gt; on the carbonyl carbon of Thr&amp;lt;sup&amp;gt;65&amp;lt;/sup&amp;gt;.&amp;lt;ref name=&amp;quot;Ormo&amp;quot; /&amp;gt;&lt;br /&gt;
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In high protein concentrations, GFP has been found to dimerize under the influence of high ionic strength between the two monomers.  In &#039;&#039;Aequorea victoria&#039;&#039;, the aequorin is able to bind to the &amp;lt;scene name=&#039;Green_Fluorescent_Protein/1gfl/1&#039; target=&#039;A&#039;&amp;gt;dimer&amp;lt;/scene&amp;gt; ([[1gfl]]), but not the monomer.  Therefore, dimerization is a very important structural feature in terms of its function, as it also assists the GFP to absorb energy at the excitation wavelength of aequorin even though GFP has only a “modest” extinction coefficient.  As a result, dimers, and often even higher &amp;lt;scene name=&#039;Green_Fluorescent_Protein/1w7s/1&#039; target=&#039;A&#039;&amp;gt;multimers&amp;lt;/scene&amp;gt; ([[1w7s]]), are predominant protein populations within the jellyfish.&amp;lt;ref name=&amp;quot;Cubitt&amp;quot;&amp;gt;[http://www.sciencedirect.com/science?_ob=ArticleURL&amp;amp;_udi=B6TCV-40W0TN7-50&amp;amp;_user=4187488&amp;amp;_coverDate=11%2F30%2F1995&amp;amp;_rdoc=1&amp;amp;_fmt=high&amp;amp;_orig=search&amp;amp;_sort=d&amp;amp;_docanchor=&amp;amp;view=c&amp;amp;_acct=C000062504&amp;amp;_version=1&amp;amp;_urlVersion=0&amp;amp;_userid=4187488&amp;amp;md5=e92730038bb92b1dfbd4af45a0283cce],Cubitt AB, Heim R, Adams SR, Boyd AE, Gross LA, Tsien R.  1995.  Understanding, improving, and using green fluorescent protein.  Trends in Biochemical Sciences.  20(11): 448-455.  DOI 0.1016/S0968-0004(00)89099-4.&amp;lt;/ref&amp;gt; &lt;br /&gt;
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{{Link Toggle FancyCartoonHighQualityView}}.&lt;br /&gt;
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== Using GFP as a Research Tool ==&lt;br /&gt;
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A description of some of the ways GFP is being used as a tool in research is at [[Green_Fluorscent_Protein:_Research_Tool]].&lt;br /&gt;
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==3D Structures of Green Fluorescent Protein==&lt;br /&gt;
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&#039;&#039;Update November 2011&#039;&#039;&lt;br /&gt;
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[[2qu1]], [[2h9w]] – jGFP - jellyfish&amp;lt;br /&amp;gt;&lt;br /&gt;
[[3la1]], [[3i19]], [[2wur]], [[3gex]], [[2qrf]], [[2qt2]], [[2qz0]], [[2gj1]], [[2gj2]], [[3cb9]], [[3cbe]], [[3cd1]], [[3cd9]], [[2hjo]], [[2hqz]], [[2hrs]], [[2okw]], [[2oky]], [[2q57]], [[2due]], [[2duf]], [[2dug]], [[2duh]], [[2dui]], [[2q6p]], [[2hcg]], [[2hfc]], [[2hgd]], [[2hgy]], [[2awj]], [[2awk]], [[2awl]], [[2awm]], [[2g16]], [[2g2s]], [[2g3d]], [[2g5z]], [[2g6e]], [[2ah8]], [[2aha]], [[2fwq]], [[2fzu]], [[2b3p]], [[2b3q]], [[1z1p]], [[1z1q]], [[1yhg]], [[1yhh]], [[1yhi]], [[1yj2]], [[1yjf]], [[1s6z]], [[1q4a]], [[1q4b]], [[1q4c]], [[1q4d]], [[1q4e]], [[1q73]], [[1qyf]], [[1qyo]], [[1qyq]], [[1qst]], [[1qy3]], [[1cv7]], [[1jc0]], [[1jc1]],  [[1jby]], [[1jbz]], [[1kp5]], [[1kyp]], [[1hcj]], [[1h6r]], [[1b9c]], [[1c4f]], [[1emc]], [[1eme]], [[1emf]], [[1emk]], [[1eml]], [[1emm]], [[2emd]], [[2emn]], [[2emo]], [[1emb]], [[1gfl]], [[1ema]], [[2y0g]], [[3gj1]], [[3gj2]], [[3p28]], [[1qxt]] – jGFP (mutant)&amp;lt;br /&amp;gt;&lt;br /&gt;
[[3evp]] – jGFP circular permutation&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2h6v]] – jGFP+imidazole derivative&amp;lt;br /&amp;gt;&lt;br /&gt;
[[1rm9]], [[1rmm]], [[1rmo]], [[1rmp]], [[1rrz]] – jGFP containing fluorotryptophan&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2o24]], [[2o29]], [[2o2b]], [[1w7u]], [[1w7t]], [[1w7s]], [[1emg]] – jGFP (mutant)+imidazole derivative&amp;lt;br /&amp;gt;&lt;br /&gt;
[[1kyr]] – jGFP (mutant)+imidazole derivative+Cu&amp;lt;br /&amp;gt;&lt;br /&gt;
[[1kys]] – jGFP (mutant)+imidazole derivative+Zn&amp;lt;br /&amp;gt;&lt;br /&gt;
[[3ogo]] – jGFP+cGFP nanobody – camel&amp;lt;br /&amp;gt;&lt;br /&gt;
[[3g9a]], [[3k1k]] – jGFP+minimize nanobody – &#039;&#039;Lama pacos&#039;&#039;&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2qle]] – GFP (mutant) – &#039;&#039;Azotobacter vinelandii&#039;&#039;&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2rh7]] – GFP – &#039;&#039;Renilla reniformis&#039;&#039;&amp;lt;br /&amp;gt;&lt;br /&gt;
[[3adf]] – monomeric azami green – &#039;&#039;Galaxea fascicularis&#039;&#039;&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2vzx]] – GFP DENDRA2 – Dendronephthya&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2gw3]] – GFP KAEDE – &#039;&#039;Trachiphyllia geoffroyi&#039;&#039;&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2pox]], [[2gx0]], [[2gx2]], [[2iov]], [[2ie2]] – FP DRONPA – Echinophyllia&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2dd7]] – CpGFP - &#039;&#039;Chiridius poppei&#039;&#039;&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2dd9]] – CpGFP (mutant)&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2c9i]] – saGFP – sea anemone&amp;lt;br /&amp;gt;&lt;br /&gt;
[[1xmz]] – saGFP (mutant)&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2c9j]] – GFP – &#039;&#039;Cerianthus membranaceus&#039;&#039;&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2hpw]] – GFP – &#039;&#039;Clytia gregaria&#039;&#039;&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2g3o]] – PpGFP – &#039;&#039;Pontellina plumata&#039;&#039;&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2g6x]], [[2g6y]] – PpGFP (mutant)&amp;lt;br /&amp;gt;&lt;br /&gt;
[[3lva]], [[3lvc]], [[3lvd]] – GFP (mutant) – &#039;&#039;Aequoarea coerulescens&#039;&#039;&amp;lt;br /&amp;gt;&lt;br /&gt;
&lt;br /&gt;
===Yellow fluorescent protein===&lt;br /&gt;
&lt;br /&gt;
[[3dpw]], [[3dpx]], [[3dpz]], [[3dq1]], [[3dq2]], [[3dq3]], [[3dq4]], [[3dq5]], [[3dq6]], [[3dq7]], [[3dq8]], [[3dq9]], [[3dqa]], [[3dqc]], [[3dqd]], [[3dqe]], [[3dqf]], [[3dqh]], [[3dqi]], [[3dqj]], [[3dqk]], [[3dql]], [[3dqm]], [[3dqn]], [[3dqo]], [[3dqu]], [[1myw]], [[1huy]], [[2yfp]], [[1yfp]] – jGFP (mutant)&amp;lt;br /&amp;gt;&lt;br /&gt;
[[1f09]], [[1f0b]] – jGFP (mutant)+imidazole derivative+I&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2ogr]] – Z-FP - Zoanthus&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2pxs]], [[2pxw]], [[1xa9]], [[1xae]] – Z-FP (mutant)&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2jad]] – jGFP/glutaredoxin&amp;lt;br /&amp;gt;&lt;br /&gt;
&lt;br /&gt;
===Red fluorescent protein===&lt;br /&gt;
&lt;br /&gt;
[[2icr]], [[2ojk]] –  Z-RFP &amp;lt;br /&amp;gt;&lt;br /&gt;
[[2fl1]] – Z-RFP (mutant)&amp;lt;br /&amp;gt;&lt;br /&gt;
[[3bx9]], [[3bxa]], [[3bxb]], [[3bxc]], [[3e5t]], [[3e5w]], [[1uis]], [[3ip2]], [[3pj5]], [[3pj7]], [[3pjb]], [[3pib]] -  EnRFP  – &#039;&#039;Entacmaea quadricolor&#039;&#039;&amp;lt;br /&amp;gt;&lt;br /&gt;
[[3e5v]], [[3rwt]] – EnRFP (mutant)&amp;lt;br /&amp;gt;&lt;br /&gt;
[[1zgo]], [[2vad]], [[2vae]], [[1ggx]] – DiRFP – &#039;&#039;Discosoma&#039;&#039;&amp;lt;br /&amp;gt;&lt;br /&gt;
[[1zgp]], [[1zgq]], [[2h8q]], [[2v4e]], [[1g7k]] – DiRFP (mutant)&amp;lt;br /&amp;gt;&lt;br /&gt;
[[3cfa]] – AsRFP – &#039;&#039;Anemonia sulcata&#039;&#039;&amp;lt;br /&amp;gt;&lt;br /&gt;
[[3nt3]], [[3nt9]] – RFP – artificial gene&amp;lt;br /&amp;gt;&lt;br /&gt;
[[1yzw]] – RFP – &#039;&#039;Heteractis&#039;&#039; &lt;br /&gt;
&lt;br /&gt;
===Cyan fluorescent protein===&lt;br /&gt;
&lt;br /&gt;
[[2wsn]], [[2wso]] - jGFP&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2otb]] – cyan C-FP – Clavularia&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2ote]] - cyan C-FP (mutant)&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2zo6]], [[2zo7]] – cyan FP – &#039;&#039;Fungia concinna&#039;&#039;&amp;lt;br /&amp;gt;&lt;br /&gt;
[[1oxd]], [[1oxe]], [[1oxf]] – cyan FP (mutant) – marker plasmid&amp;lt;br /&amp;gt;&lt;br /&gt;
&lt;br /&gt;
===Blue fluorescent protein===&lt;br /&gt;
&lt;br /&gt;
[[1bfp]] – jGFP (mutant)&lt;br /&gt;
&lt;br /&gt;
===Photoconvertible fluorescent protein===&lt;br /&gt;
&lt;br /&gt;
[[2vvh]], [[2vvi]], [[2vvj]], [[3p8u]] –  LhGFP (mutant) – &#039;&#039;Lobophyllia hemprichii&#039;&#039;&amp;lt;br /&amp;gt;&lt;br /&gt;
[[1zux]] –  LhGFP&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2btj]] -  LhGFP+imidazole derivative&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2ddc]], [[1xss]] –  FfFP – &#039;&#039;Favia favus&#039;&#039;&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2ddd]] -  FfFP (mutant)&amp;lt;br /&amp;gt;&lt;br /&gt;
[[3cff]], [[3cfh]] – AsGFP (mutant)&lt;br /&gt;
&lt;br /&gt;
===Green fluorescent protein chimera===&lt;br /&gt;
&lt;br /&gt;
[[3ai4]] – jGFP/mPolymerase iota ubiquitin binding motif - mouse&amp;lt;br /&amp;gt;&lt;br /&gt;
[[3ai5]] - jGFP/m ubiquitin&amp;lt;br /&amp;gt;&lt;br /&gt;
[[3o77]], [[3o78]], [[3ek4]], [[3ek7]] - jGFP/myosin light chain kinase/calmodulin&amp;lt;br /&amp;gt;&lt;br /&gt;
[[3evr]], [[3evu]], [[3evv]] - jGFP/myosin light chain kinase/calmodulin+Ca&amp;lt;br /&amp;gt;&lt;br /&gt;
[[3ek8]], [[3ekh]], [[3ekj]] - jGFP/myosin light chain kinase/calmodulin (mutant)&amp;lt;br /&amp;gt;&lt;br /&gt;
[[3osq]], [[3osr]] – jGFP/maltose-binding protein&lt;br /&gt;
 &lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
==Reference for this Structure==&lt;br /&gt;
&lt;br /&gt;
Ormo M, Cubitt AB, Kallio K, Gross LA, Tsien RY, Remington SJ.  1996.  Crystal structure of the &#039;&#039;Aequorea victoria&#039;&#039; green fluorescent protein.  Science.  273(5280):1392-1395.  [http://www.sciencemag.org/cgi/content/abstract/273/5280/1392 DOI 10.1126/science.273.5280.1392].&lt;br /&gt;
&lt;br /&gt;
==References==&lt;br /&gt;
&lt;br /&gt;
{{Reflist}}&lt;br /&gt;
&lt;br /&gt;
==Additional Resources==&lt;br /&gt;
*For additional information, see: [[Colored &amp;amp; Bioluminescent Proteins]]&lt;br /&gt;
*[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ema First Glance]&lt;br /&gt;
*PDBsum: [http://www.ebi.ac.uk/pdbsum/1ema 1ema]&lt;br /&gt;
*RCSB PDB [http://www.rcsb.org/pdb/explore.do?structureId=1ema 1ema]&lt;br /&gt;
*[http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ema OCA]&lt;br /&gt;
*UniProt: [http://www.uniprot.org/uniprot/P42212 P42212]&lt;br /&gt;
*Scop: [http://scop.mrc-lmb.cam.ac.uk/scop/data/scop.b.e.gc.b.b.b.html P42212]&lt;br /&gt;
*CATH: [http://www.cathdb.info/domain/1emaA00 1emaA00]&lt;br /&gt;
*Pfam: [http://pfam.sanger.ac.uk/family?acc=PF01353 PF01353]&lt;br /&gt;
*InterPro: [http://www.ebi.ac.uk/interpro/ISearch?query=IPR000786 IPR000786]&lt;br /&gt;
*[http://www.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb42_1.html GFP featured] at the &#039;&#039;&#039;[http://www.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month]&#039;&#039;&#039; series of tutorials by [[User:David_S._Goodsell|David Goodsell]].&lt;br /&gt;
* [http://www.nature.com/nature/journal/v462/n7270/edsumm/e091112-05.html Inside green fluorescent protein] - editor&#039;s summary that accompanied [http://www.nature.com/nature/journal/v462/n7270/covers/ structural detail of GFP chromophore on the cover] of Nature.&lt;br /&gt;
&lt;br /&gt;
[[he:GFP_(Hebrew)]]&lt;br /&gt;
&lt;br /&gt;
[[Category:Topic Page]]&lt;/div&gt;</summary>
		<author><name>Jing Liu</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1329551</id>
		<title>User:Jing Liu/Sandbox 1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1329551"/>
		<updated>2011-12-07T17:30:01Z</updated>

		<summary type="html">&lt;p&gt;Jing Liu: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;applet load=&#039;1ema&#039; size=&#039;450&#039; frame=&#039;true&#039; align=&#039;right&#039; scene=&#039;Green_Fluorescent_Protein/1ema_gfp_default/2&#039; caption=&#039;Green fluorescent protein complex with peptide-derived chromophore ([[1ema]])&#039; /&amp;gt; &lt;br /&gt;
&#039;&#039;&#039;Green fluorescent protein (GFP)&#039;&#039;&#039; is a [[bioluminescent]] polypeptide consisting of 238 residues isolated from the body of [[Aequorea victoria]] jellyfish.&amp;lt;ref name=&amp;quot;PDBsum&amp;quot;&amp;gt;[http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=1ema&amp;amp;template=main.html], Protein Database (PDBsum): 1ema.  European Bioinformatics (EBI); 2009.&amp;lt;/ref&amp;gt; GFP converts the blue chemiluminescent of [[aequorin]] in the jellyfish into green fluorescent light.&amp;lt;ref name=&amp;quot;Yang&amp;quot;&amp;gt;[http://www-bioc.rice.edu/Bioch/Phillips/Papers/gfpbio.html], Yang F, Moss LG, Phillips GN Jr.  1996.  The molecular structure of green fluorescent protein.  Biotechnology.  14: 1246-1251.  DOI 10.1038/nbt1096-1246.&amp;lt;/ref&amp;gt; It remains unclear why these jellyfish use fluorescence, why green is better than blue, or why they produce a separate protein for green fluorescence as opposed to simply mutating the present aequorin to shift its wavelength,&amp;lt;ref name=&amp;quot;Tsien&amp;quot; /&amp;gt; but in the laboratory, GFP can be incorporated into a variety of biological systems in order to function as a marker protein. Since its discovery in 1962, GFP has become a significant contributor to the research of monitoring gene expression, localization, mobility, traffic, interactions between various membrane and cytoplasmic proteins, as well as many others.&amp;lt;ref name=&amp;quot;Haldar&amp;quot;&amp;gt;[http://www.springerlink.com/content/wvg513864266g77n/fulltext.pdf], Haldar S, Chattopadhyay A.  2009.  The green journey.  J Fluoresc.  19:1-2.  DOI 10.1007/s10895-008-0455-6; biographical background on [http://en.wikipedia.org/wiki/Douglas_Prasher Douglas Prasher], [http://en.wikipedia.org/wiki/Martin_Chalfie Martin Chalfie] and [http://en.wikipedia.org/wiki/Roger_Tsien Roger Tsien].&amp;lt;/ref&amp;gt;&lt;br /&gt;
&lt;br /&gt;
==History==&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;Aequorea victoria&#039;&#039; was first discovered and investigated for its bioluminescence by Frank Johnson, who invited Osamu Shimomura to work with him in on a small island not far from British Columbia, where the jellyfish is abundant.&amp;lt;ref name=&amp;quot;Shimomura&amp;quot;&amp;gt;[http://nobelprize.org/nobel_prizes/chemistry/laureates/2008/shimomura_lecture.pdf], Shimomura O.  The discovery of green fluorescent protein.  Nobel Prize Lecture; 2009;; biographical background at [http://en.wikipedia.org/wiki/Osamu_Shimomura Wikipedia].&amp;lt;/ref&amp;gt; Found off the west coast of the United States between British Columbia and central California,&amp;lt;ref name=&amp;quot;Cowles&amp;quot;&amp;gt;[http://www.wallawalla.edu/academics/departments/biology/rosario/inverts/Cnidaria/Class-Hydrozoa/Hydromedusae/Aequorea_victoria.html],Cowles D, Cowles J.  &#039;&#039;Aequorea victoria&#039;&#039;.  2007.  Walla Wall University.&amp;lt;/ref&amp;gt; the jellyfish was considered a local phenomenon as it would drift in and out of the harbors.&amp;lt;ref name=&amp;quot;Shimomura&amp;quot; /&amp;gt;&lt;br /&gt;
[[Image:GFP mice.png|thumb|left|450x200px|Mice with GFP inserted into their genomes for neurology studies.]]&lt;br /&gt;
&lt;br /&gt;
Shimomura was originally looking only to isolate the blue luminescent protein of &#039;&#039;Aequorea victoria&#039;&#039;, traditionally thought to be [[luciferase]], but it would soon become apparent that the glow was in fact due to aequorin, a substance related, but slightly varying from luciferase.&amp;lt;ref name=&amp;quot;Haldar&amp;quot; /&amp;gt;&amp;lt;ref name=&amp;quot;Shimomura&amp;quot; /&amp;gt; However, the light emitted from aequorin still differed from the light emitted from the wild jellyfish. This quandary led to the discovery of the green fluorescent protein responsible for this disparity, but sufficient amounts of the protein could not be collected for study until 1979. The journey to discover the nature of GFP had begun.&amp;lt;ref name=&amp;quot;Shimomura&amp;quot; /&amp;gt;&lt;br /&gt;
&lt;br /&gt;
In the 1990’s, Douglas Prasher, Frank Predergast, and co-workers successfully cloned the gene that encoded for GFP.  Martin Chalfie further pursued this line of work and was eventually able to express GFP in heterologous systems such as E. coli and C. elegans.  Chalfie’s research provided the first evidence that GFP was unique as it did not require the presence of any exogenous substance or cofactor for fluorescence.&amp;lt;ref name=&amp;quot;Haldar&amp;quot; /&amp;gt; The lack for the need for a cofactor proved that the cloned GFP gene contained all the information necessary for posttranslational synthesis of the chromophore. &amp;lt;ref name=&amp;quot;Tsien&amp;quot; /&amp;gt;&lt;br /&gt;
&lt;br /&gt;
Roger Tsien and co-workers were intrigued by the absence of a necessary cofactor and began to research the structure of GFP and how it relates to its fluorescence.  They discovered that a helix within the beta barrel structure of GFP actually contained a fluorophore responsible for fluorescence.  In researching its structure, they were able to develop GFP derivatives with improved fluorescence and photo-stability.  Shimomura, Chalfie, and Tsien were each recognized for their work involving GFP with the Nobel Prize in 2008.&amp;lt;ref name=&amp;quot;Haldar&amp;quot; /&amp;gt;  In the time since the work of these three researchers, GFP has been successfully expressed and utilized in bacteria, yeast, slime mold, plants, drosophila fruit flies, zebra-fish, and mammalian cells.&amp;lt;ref name=&amp;quot;Yang&amp;quot; /&amp;gt;  Below, mice have had GFP inserted into their genomes for studies in neurology.&lt;br /&gt;
&lt;br /&gt;
==Structure==&lt;br /&gt;
&lt;br /&gt;
===Primary &amp;amp; Secondary Structure===&lt;br /&gt;
{{STRUCTURE_1ema |  SIZE=400 |PDB=1ema  |  SCENE=Green_Fluorescent_Protein/1ema_gfp_default/2 |CAPTION = 1ema, resolution 1.90&amp;amp;Aring; (&amp;lt;scene name=&#039;Green_Fluorescent_Protein/1ema_gfp_default/2&#039;&amp;gt;default scene&amp;lt;/scene&amp;gt;).}}&lt;br /&gt;
Green fluorescent protein (&amp;lt;scene name=&#039;Green_Fluorescent_Protein/1ema_gfp_default/2&#039;&amp;gt;default scene&amp;lt;/scene&amp;gt;) is a 21 kDa protein consisting of 238 residues strung together&amp;lt;ref&amp;gt;Primary structure at [http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=1ema&amp;amp;template=protein.html&amp;amp;r=wiring&amp;amp;l=1&amp;amp;chain=A www.ebi.aci.uk].&amp;lt;/ref&amp;gt; to form a  &lt;br /&gt;
&amp;lt;scene name=&#039;Green_Fluorescent_Protein/1ema_gfp_barrel/2&#039;&amp;gt;secondary structure&amp;lt;/scene&amp;gt; of five α-helices and one eleven-stranded β-pleated sheet,&amp;lt;ref name=&amp;quot;PDBsum&amp;quot; /&amp;gt; where each strand contains nine to thirteen residues each.&amp;lt;ref name=&amp;quot;Ormo&amp;quot; /&amp;gt;  (To view the primary and secondary structure of GFP, go to .)  These β-strands display an almost “seamless symmetry” in which only two of the strands vary in structural content.&amp;lt;ref name=&amp;quot;Phillips&amp;quot;&amp;gt;PMID: 9434902&amp;lt;/ref&amp;gt;  This β-sheet conforms itself through regular hydrogen bonding into a β-barrel.&amp;lt;ref name=&amp;quot;Yang&amp;quot; /&amp;gt;  In GFP, the structure is so regular that &amp;lt;scene name=&#039;Green_Fluorescent_Protein/Water_stripes/1&#039;&amp;gt;&amp;quot;stripes&amp;quot;&amp;lt;/scene&amp;gt; of water molecules (red) can be seen following the structure of the barrel.&amp;lt;ref name=&amp;quot;Phillips&amp;quot; /&amp;gt;  Together with the α-helices at either end of the molecule, a nearly perfect cylinder is produced, 42Å long and 24Å in diameter,&amp;lt;ref name=&amp;quot;Ormo&amp;quot; /&amp;gt; creating what is referred to as a “β-can” formation.&amp;lt;ref name=&amp;quot;Phillips&amp;quot; /&amp;gt;  The short helical segments at either end of the cylinder form “caps” to further protect the interior of the β-barrel.&amp;lt;ref name=&amp;quot;Phillips&amp;quot; /&amp;gt;  Overall stability is maintained by this β-can structure, helping to resist unfolding from heat and other denaturants.&amp;lt;ref name=&amp;quot;Yang&amp;quot; /&amp;gt;&lt;br /&gt;
&lt;br /&gt;
One &amp;lt;scene name=&#039;Green_Fluorescent_Protein/Central_helix/1&#039;&amp;gt;α-helix&amp;lt;/scene&amp;gt; can be found running through the central axis of the β-barrel,&amp;lt;ref name=&amp;quot;Haldar&amp;quot; /&amp;gt; roughly &amp;lt;scene name=&#039;Green_Fluorescent_Protein/Perpendicular/1&#039;&amp;gt;perpendicular&amp;lt;/scene&amp;gt; to the symmetry axis of the barrel.&amp;lt;ref name=&amp;quot;Ormo&amp;quot;&amp;gt;Ormo M, Cubitt AB, Kallio K, Gross LA, Tsien RY, Remington SJ.  1996.  Crystal structure of the &#039;&#039;Aequorea victoria&#039;&#039; green fluorescent protein.  Science.  273(5280):1392-1395.  DOI 10.1126/science.273.5280.1392.&amp;lt;/ref&amp;gt;  This helix is extremely important as it contains the fluorophore responsible for fluorescence.&amp;lt;ref name=&amp;quot;Yang&amp;quot; /&amp;gt;&amp;lt;ref name=&amp;quot;Haldar&amp;quot; /&amp;gt;  This α-helix in particular is highly stabilized by the many &amp;lt;scene name=&#039;Green_Fluorescent_Protein/Spacefill/1&#039;&amp;gt;contacts&amp;lt;/scene&amp;gt; that are made with each strand of the barrel.&amp;lt;ref name=&amp;quot;Andrews&amp;quot;&amp;gt;PMID:18713871&amp;lt;/ref&amp;gt;&lt;br /&gt;
&lt;br /&gt;
{{Link Toggle FancyCartoonHighQualityView}}.&lt;br /&gt;
&lt;br /&gt;
===The Chromophore===&lt;br /&gt;
&lt;br /&gt;
The &amp;lt;scene name=&#039;Green_Fluorescent_Protein/Chromophore/1&#039;&amp;gt;chromophore&amp;lt;/scene&amp;gt; (&amp;lt;scene name=&#039;Green_Fluorescent_Protein/1ema_gfp_chromophorezoom/6&#039;&amp;gt;top view&amp;lt;/scene&amp;gt;) of GFP is located at the center of the β-barrel with a wild-type excitation peak of 395 nm, and a minor peak at 475 nm (about three times less intense&amp;lt;ref name=&amp;quot;Tsien&amp;quot; /&amp;gt;) &amp;lt;ref name=&amp;quot;Yang&amp;quot; /&amp;gt;&amp;lt;ref name=&amp;quot;Cubitt&amp;quot; /&amp;gt;&amp;lt;ref name=&amp;quot;Ormo&amp;quot; /&amp;gt;&amp;lt;ref name=&amp;quot;Phillips&amp;quot; /&amp;gt; with extinction coefficients of approximately 30,000 and 7,000 M&amp;lt;sup&amp;gt;-1&amp;lt;/sup&amp;gt; cm&amp;lt;sup&amp;gt;-1&amp;lt;/sup&amp;gt;, respectively.&amp;lt;ref name=&amp;quot;Yang&amp;quot; /&amp;gt;&amp;lt;ref name=&amp;quot;Phillips&amp;quot; /&amp;gt;  Interestingly, the &#039;&#039;Aequorea victoria&#039;&#039; jellyfish utilizes the smaller of the two excitation peaks as pure aequorin emits a light of 470 nm.&amp;lt;ref name=&amp;quot;Tsien&amp;quot;&amp;gt;Tsien, Roger Y.  1998.  The Green Fluorescent Protein.  Annual Review in Biochemistry.  67:509-544.&amp;lt;/ref&amp;gt;  The relative amplitudes of these two excitation peaks can vary depending on environmental factors and previous illumination.&amp;lt;ref name=&amp;quot;Ormo&amp;quot; /&amp;gt;  For example, continued excitation leads to a diminution of the 395 nm excitation peak with a reciprocal amplification of the 475 nm peak.&amp;lt;ref name=&amp;quot;Phillips&amp;quot; /&amp;gt;  Regardless of absorption, the chromophore of GFP emits light of 508 nm.&amp;lt;ref name=&amp;quot;Yang&amp;quot; /&amp;gt;&amp;lt;ref name=&amp;quot;Cubitt&amp;quot; /&amp;gt;&amp;lt;ref name=&amp;quot;Ormo&amp;quot; /&amp;gt;&amp;lt;ref name=&amp;quot;Phillips&amp;quot; /&amp;gt;  &lt;br /&gt;
&lt;br /&gt;
Three amino residues in the central α-helix constitute the fluorophore of GFP: Ser&amp;lt;sup&amp;gt;65&amp;lt;/sup&amp;gt;Tyr&amp;lt;sup&amp;gt;66&amp;lt;/sup&amp;gt;Gly&amp;lt;sup&amp;gt;67&amp;lt;/sup&amp;gt; (see below).  Tsien et al. discovered that this tri-peptide sequence is post-translationally modified by internal cyclization and oxidation&amp;lt;ref name=&amp;quot;Haldar&amp;quot; /&amp;gt; to produce a &amp;lt;scene name=&#039;Green_Fluorescent_Protein/Chromophore_structure/1&#039;&amp;gt;4-(p-hydroxybenzylidene)-imidazolidin-5-one&amp;lt;/scene&amp;gt; structure.&amp;lt;ref name=&amp;quot;Yang&amp;quot; /&amp;gt;  Studies with E. coli proposed a sequential mechanism for the formation of the fluorophore that was initiated by a rapid cyclization between Ser&amp;lt;sup&amp;gt;65&amp;lt;/sup&amp;gt; and Gly&amp;lt;sup&amp;gt;67&amp;lt;/sup&amp;gt; to form an imidazolin-5-one intermediate.&amp;lt;ref name=&amp;quot;Yang&amp;quot; /&amp;gt;  This rapid cyclization is carried out via nucleophilic attack of the amino group from Gly&amp;lt;sup&amp;gt;67&amp;lt;/sup&amp;gt; on the carbonyl group of Ser&amp;lt;sup&amp;gt;65&amp;lt;/sup&amp;gt; to form a five-membered ring.  The loss of water then forms the imidazolin-5-one intermediate.&amp;lt;ref name=&amp;quot;Cubitt&amp;quot; /&amp;gt;  Cyclization is succeeded by a much slower rate-limiting oxygenation of the Tyr&amp;lt;sup&amp;gt;66&amp;lt;/sup&amp;gt; hydroxybenzyl side chain by atmospheric oxygen (No fluorescence was seen in anaerobically grown E. coli.), resulting in the 4-(p-hydroxybenzylidene)-imidazolidin-5-one stucture.&amp;lt;ref name=&amp;quot;Yang&amp;quot; /&amp;gt;&amp;lt;ref name=&amp;quot;Cubitt&amp;quot; /&amp;gt;&amp;lt;ref name=&amp;quot;Phillips&amp;quot; /&amp;gt;  The double bond that results from this series of reactions results in the linkage of the two π-systems of the rings, forming a larger conjugated system essential for fluorophore stability. &amp;lt;ref name=&amp;quot;Bublitz&amp;quot;&amp;gt; Bublitz G, King BA, Boxer SG.  1998.  Electronic structure of the chromophore in green fluorescent protein (GFP).  Journal of the American Chemical Society.  120(36): 9370-9371.  DOI 10.1021/ja98160e.&amp;lt;/ref&amp;gt;&lt;br /&gt;
[[Image:GFP Chromophore.png|center|489x360px]]&lt;br /&gt;
&lt;br /&gt;
The process is completely auto-catalytic such that there are no known co-factors or enzymatic components required.&amp;lt;ref name=&amp;quot;Yang&amp;quot; /&amp;gt;  Despite the stability of the final product, while the chromophore is forming, the environmental temperature cannot drop below 30°C or the yield of viable GFP will decrease substantially.&amp;lt;ref name=&amp;quot;Yang&amp;quot; /&amp;gt;&amp;lt;ref name=&amp;quot;Phillips&amp;quot; /&amp;gt;  This, of course, is not an issue for the protein in nature as the jellyfish is unlikely to encounter waters of this degree in the Pacific Northwest.&amp;lt;ref name=&amp;quot;Tsien&amp;quot; /&amp;gt;  Such a temperature sensitivity is only relevant during formation as the stability of the final product is maintained through a network of close contacts surrounding the fluorophore.&amp;lt;ref name=&amp;quot;Yang&amp;quot; /&amp;gt;  This, however, can and has been used in [[pulse-chase experiments]] in which the GFP-expressing cells are exposed to varying temperatures in place of labeled vs. unlabeled trials.&amp;lt;ref name=&amp;quot;Tsien&amp;quot; /&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;applet load=&#039;1ema&#039; size=&#039;500&#039; frame=&#039;true&#039; align=&#039;right&#039; scene=&#039;Green_Fluorescent_Protein/Polar_interactions/2&#039; name=&#039;2&#039;/&amp;gt;&lt;br /&gt;
&lt;br /&gt;
As the central α-helix is not located directly in the center of the β-barrel, cavities of differing area exist on either side of the chromophore.  The larger cavity, consisting of about 135 Å,&amp;lt;ref name=&amp;quot;Ormo&amp;quot; /&amp;gt; does not open out to the bulk solvent, but rather houses &amp;lt;scene name=&#039;Green_Fluorescent_Protein/Water_molecules/1&#039;&amp;gt;four water molecules&amp;lt;/scene&amp;gt;.&amp;lt;ref name=&amp;quot;Ormo&amp;quot; /&amp;gt;&amp;lt;ref name=&amp;quot;Van&amp;quot;&amp;gt;van Thor JJ, Sage, JT.  2006.  Charge transfer in green fluorescent protein.  Photochemical &amp;amp; Photobiological Sciences.  5:597-602.  DOI 10.1039/b516525c.&amp;lt;/ref&amp;gt;  Had this space not been occupied, it would be expected to considerably destabilize the protein as a whole.  The hydrogen bonding created by the presence of the water molecules, however, helps to link the buried &amp;lt;scene name=&#039;Green_Fluorescent_Protein/Gln69_glu222/1&#039; target=&#039;2&#039;&amp;gt;side chains&amp;lt;/scene&amp;gt; of Glu&amp;lt;sup&amp;gt;222&amp;lt;/sup&amp;gt; and Gln&amp;lt;sup&amp;gt;69&amp;lt;/sup&amp;gt; that would otherwise be actively polar.&amp;lt;ref name=&amp;quot;Ormo&amp;quot; /&amp;gt;  Therefore, the water molecules are extremely important in establishing a hydrogen bonding network about the chromophor.&amp;lt;ref name=&amp;quot;Lammich&amp;quot;&amp;gt;PMID: 17040991&amp;lt;/ref&amp;gt;&lt;br /&gt;
&lt;br /&gt;
The opposite side of the chromophore, however, is within close proximity of several aromatic and polar side chains.  Several &amp;lt;scene name=&#039;Green_Fluorescent_Protein/Polar_interactions/2&#039;&amp;gt;polar interactions&amp;lt;/scene&amp;gt; between the surrounding residues and the chromophore are present including: hydrogen bonds of His&amp;lt;sup&amp;gt;148&amp;lt;/sup&amp;gt;, Thr&amp;lt;sup&amp;gt;203&amp;lt;/sup&amp;gt;, and Ser&amp;lt;sup&amp;gt;205&amp;lt;/sup&amp;gt; with the phenolic hydroxyl of Tyr&amp;lt;sup&amp;gt;66&amp;lt;/sup&amp;gt;; Arg&amp;lt;sup&amp;gt;96&amp;lt;/sup&amp;gt; and Gln&amp;lt;sup&amp;gt;94&amp;lt;/sup&amp;gt; with the carbonyl of the imidazolidinone ring; and hydrogen bonds of Glu&amp;lt;sup&amp;gt;222&amp;lt;/sup&amp;gt; with the side chain of Thr&amp;lt;sup&amp;gt;65&amp;lt;/sup&amp;gt;.  Additional hydrogen bonding in the area around the chromophore helps to stabilize Arg&amp;lt;sup&amp;gt;96&amp;lt;/sup&amp;gt; in the protonated form, which suggests the presence of a partial negative charge on the carbonyl oxygen of the imidazolidinone ring in the deprotonated fluorophore.&amp;lt;ref name=&amp;quot;Ormo&amp;quot; /&amp;gt;  Arg&amp;lt;sup&amp;gt;96&amp;lt;/sup&amp;gt; and Gln&amp;lt;sup&amp;gt;94&amp;lt;/sup&amp;gt; in turn help to steady the imidazolidone.&amp;lt;ref name=&amp;quot;Yang&amp;quot; /&amp;gt;  Therefore, it is thought that Arg&amp;lt;sup&amp;gt;96&amp;lt;/sup&amp;gt; is essential for the formation of the fluorophore by catalyzing the initial ring closure.&amp;lt;ref name=&amp;quot;Ormo&amp;quot; /&amp;gt;  Tyr&amp;lt;sup&amp;gt;145&amp;lt;/sup&amp;gt; provides a stabilizing &lt;br /&gt;
&amp;lt;scene name=&#039;Green_Fluorescent_Protein/Edge_face_interaction/1&#039;&amp;gt;edge-face interaction&amp;lt;/scene&amp;gt;&amp;lt;ref&amp;gt; [http://www.tim.hi-ho.ne.jp/dionisio/ Information about edge-face (CH/π) interactions].&amp;lt;/ref&amp;gt; with the benzyl ring of the chromophore.&amp;lt;ref name=&amp;quot;Ormo&amp;quot; /&amp;gt;  The stability provided by the internal polar interactions are further augmented by the surrounding β-barrel.  &lt;br /&gt;
&lt;br /&gt;
The β-barrel provides a highly constrained environment that protects the chromophore from the bulk solvent,&amp;lt;ref name=&amp;quot;Haldar&amp;quot; /&amp;gt; nearly creating the atmosphere of a vacuum.&amp;lt;ref name=&amp;quot;Lammich&amp;quot; /&amp;gt;  This is most likely responsible for the small [[Stoke’s shift]], or the small wavelength difference between excitation and emission.&amp;lt;ref name=&amp;quot;Ormo&amp;quot; /&amp;gt;  &lt;br /&gt;
&lt;br /&gt;
{{Link Toggle FancyCartoonHighQualityView}}.&lt;br /&gt;
&lt;br /&gt;
Findings show that fluorescence will not occur from a naked chromophore, but rather requires the protection of the β-can structure.&amp;lt;ref name=&amp;quot;Cubitt&amp;quot; /&amp;gt;  However, &#039;&#039;in crystallum&#039;&#039; GFP will exhibit a nearly identical fluorescence spectrum and lifetime when compared with aqueous GFP.  These two elements point to a fluorescence that is not inherent to the isolated fluorophore,&amp;lt;ref name=&amp;quot;Yang&amp;quot; /&amp;gt;&amp;lt;ref name=&amp;quot;Phillips&amp;quot; /&amp;gt; but rather from the auto-catalytic cyclization of the polypeptide sequence Ser&amp;lt;sup&amp;gt;65&amp;lt;/sup&amp;gt;Tyr&amp;lt;sup&amp;gt;66&amp;lt;/sup&amp;gt;Gly&amp;lt;sup&amp;gt;67&amp;lt;/sup&amp;gt; and subsequent oxidation of Tyr&amp;lt;sup&amp;gt;66&amp;lt;/sup&amp;gt;.&amp;lt;ref name=&amp;quot;Phillips&amp;quot; /&amp;gt;  However, this sequence is found in many proteins - why does GFP fluoresce?  According to Phillips (1997), fluorophore formation is due to the close proximity of the backbone atoms between Ser&amp;lt;sup&amp;gt;65&amp;lt;/sup&amp;gt;. and Gly&amp;lt;sup&amp;gt;67&amp;lt;/sup&amp;gt; gained through a lack of sterical hindrance by the hydrogen atom side chain of glycine.  In fact, no functional fluorescent proteins have been found in which any other amino acid other than glycine was found at position 67.  Even so, there are still proteins that have this specific sequence, therefore, there must be another inherent property to GFP that is still left misunderstood.&amp;lt;ref name=&amp;quot;Phillips&amp;quot; /&amp;gt;  &lt;br /&gt;
&lt;br /&gt;
This quandary led Phillips to study the acid/base chemistry catalyzing the initial cyclization of the chromophore.  He found that Arg&amp;lt;sup&amp;gt;96&amp;lt;/sup&amp;gt; actually acts as a &lt;br /&gt;
&amp;lt;scene name=&#039;Green_Fluorescent_Protein/Arg96/1&#039; target=&#039;2&#039; &amp;gt;base&amp;lt;/scene&amp;gt; by withdrawing electrons through hydrogen bonding with the carbonyl oxygen of Ser&amp;lt;sup&amp;gt;65&amp;lt;/sup&amp;gt; to activate the carbonyl carbon for nucleophilic attack by the amide nitrogen of Gly&amp;lt;sup&amp;gt;67&amp;lt;/sup&amp;gt;.  This mechanism was further supported by &#039;&#039;ab initio&#039;&#039; calculations, as well as database searches of similar compounds and protein sequences.  Through acid/base chemistry, the chromophore is stabilized by resonance.&amp;lt;ref name=&amp;quot;Phillips&amp;quot; /&amp;gt;  Femtosecond Raman spectroscopy has been used to map the alteration of the structure close the chromophore during excited-state protein transfer and shown that chromophore wagging is orchestrated by the protein environment.&amp;lt;ref name=&amp;quot;Fang&amp;quot;&amp;gt;PMID: 19907490&amp;lt;/ref&amp;gt;&lt;br /&gt;
&lt;br /&gt;
===Mutant Studies===&lt;br /&gt;
&lt;br /&gt;
&amp;lt;applet load=&#039;1ema&#039; size=&#039;400&#039; frame=&#039;true&#039; align=&#039;right&#039; scene=&#039;Green_Fluorescent_Protein/1ema_gfp_barrel/2&#039; name=&#039;A&#039;/&amp;gt;&lt;br /&gt;
Many mutant green fluorescent proteins have been developed in order to further understand the structure and mechanism of the fluorophore.  The first mutagenesis studies simply &lt;br /&gt;
&amp;lt;scene name=&#039;Green_Fluorescent_Protein/Truncated_ends/2&#039; target=&#039;A&#039;&amp;gt;truncated the ends&amp;lt;/scene&amp;gt; of the amino acid sequence (&amp;lt;scene name=&#039;Green_Fluorescent_Protein/1ema_gfp_barrel/2&#039; target=&#039;A&#039;&amp;gt;see without truncated ends&amp;lt;/scene&amp;gt;.  NOTE: The structure represented here is already truncated at the carbonyl terminus).  Shortening the polypeptide by more than seven amino acids from either terminus lead to a total loss of fluorescence, as well as a complete failure to absorb light at the traditional wavelengths.   This is most likely due to the structure of the protein.  The last seven amino acid residues of the carboxyl terminus are roughly disordered, and thus do not interfere with the overall structure.  After seven residues, however, the capping α-helix structure is disrupted, leading to an unstable or unformed chromophore.  The &amp;lt;scene name=&#039;Green_Fluorescent_Protein/Amino_terminus/2&#039; target=&#039;A&#039;&amp;gt;amino terminus&amp;lt;/scene&amp;gt; is less understood, but the same principle still applies even though the β-barrel does not begin until residue ten or eleven.&amp;lt;ref name=&amp;quot;Yang&amp;quot; /&amp;gt;  &lt;br /&gt;
&lt;br /&gt;
Point mutations have also been extensively studied in order to examine their effects on the chromophore.  In general, most point mutations lead to a diminished excitation, especially in regions of the sequence adjacent to the fluorophore or those that interact with the fluorophore.  An exception to this trend is the Ser&amp;lt;sup&amp;gt;65&amp;lt;/sup&amp;gt;Thr&amp;lt;sup&amp;gt;66&amp;lt;/sup&amp;gt; mutant (normal Ser&amp;lt;sup&amp;gt;65&amp;lt;/sup&amp;gt;Tyr&amp;lt;sup&amp;gt;66&amp;lt;/sup&amp;gt;), which actually increases fluorescence intensity, although the reason is unclear.&amp;lt;ref name=&amp;quot;Yang&amp;quot; /&amp;gt;&lt;br /&gt;
&lt;br /&gt;
An interesting mutation discovered by Ormo et al. (1996) was the Thr&amp;lt;sup&amp;gt;65&amp;lt;/sup&amp;gt;Tyr&amp;lt;sup&amp;gt;66&amp;lt;/sup&amp;gt;Gly&amp;lt;sup&amp;gt;67&amp;lt;/sup&amp;gt; mutant, which produces an α-helical conformation in the chromophore opposed to the normal conformation, which is nearly perpendicular to the helical axis, due to its interaction with Arg&amp;lt;sup&amp;gt;96&amp;lt;/sup&amp;gt;.  This further supports the idea that Arg&amp;lt;sup&amp;gt;96&amp;lt;/sup&amp;gt; is an important factor in the structural arrangement required for cyclization, perhaps by promoting the attack of Gly&amp;lt;sup&amp;gt;67&amp;lt;/sup&amp;gt; on the carbonyl carbon of Thr&amp;lt;sup&amp;gt;65&amp;lt;/sup&amp;gt;.&amp;lt;ref name=&amp;quot;Ormo&amp;quot; /&amp;gt;&lt;br /&gt;
&lt;br /&gt;
In high protein concentrations, GFP has been found to dimerize under the influence of high ionic strength between the two monomers.  In &#039;&#039;Aequorea victoria&#039;&#039;, the aequorin is able to bind to the &amp;lt;scene name=&#039;Green_Fluorescent_Protein/1gfl/1&#039; target=&#039;A&#039;&amp;gt;dimer&amp;lt;/scene&amp;gt; ([[1gfl]]), but not the monomer.  Therefore, dimerization is a very important structural feature in terms of its function, as it also assists the GFP to absorb energy at the excitation wavelength of aequorin even though GFP has only a “modest” extinction coefficient.  As a result, dimers, and often even higher &amp;lt;scene name=&#039;Green_Fluorescent_Protein/1w7s/1&#039; target=&#039;A&#039;&amp;gt;multimers&amp;lt;/scene&amp;gt; ([[1w7s]]), are predominant protein populations within the jellyfish.&amp;lt;ref name=&amp;quot;Cubitt&amp;quot;&amp;gt;[http://www.sciencedirect.com/science?_ob=ArticleURL&amp;amp;_udi=B6TCV-40W0TN7-50&amp;amp;_user=4187488&amp;amp;_coverDate=11%2F30%2F1995&amp;amp;_rdoc=1&amp;amp;_fmt=high&amp;amp;_orig=search&amp;amp;_sort=d&amp;amp;_docanchor=&amp;amp;view=c&amp;amp;_acct=C000062504&amp;amp;_version=1&amp;amp;_urlVersion=0&amp;amp;_userid=4187488&amp;amp;md5=e92730038bb92b1dfbd4af45a0283cce],Cubitt AB, Heim R, Adams SR, Boyd AE, Gross LA, Tsien R.  1995.  Understanding, improving, and using green fluorescent protein.  Trends in Biochemical Sciences.  20(11): 448-455.  DOI 0.1016/S0968-0004(00)89099-4.&amp;lt;/ref&amp;gt; &lt;br /&gt;
&lt;br /&gt;
{{Link Toggle FancyCartoonHighQualityView}}.&lt;br /&gt;
&lt;br /&gt;
== Using GFP as a Research Tool ==&lt;br /&gt;
&lt;br /&gt;
A description of some of the ways GFP is being used as a tool in research is at [[Green_Fluorscent_Protein:_Research_Tool]].&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
==3D Structures of Green Fluorescent Protein==&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;Update November 2011&#039;&#039;&lt;br /&gt;
&lt;br /&gt;
[[2qu1]], [[2h9w]] – jGFP - jellyfish&amp;lt;br /&amp;gt;&lt;br /&gt;
[[3la1]], [[3i19]], [[2wur]], [[3gex]], [[2qrf]], [[2qt2]], [[2qz0]], [[2gj1]], [[2gj2]], [[3cb9]], [[3cbe]], [[3cd1]], [[3cd9]], [[2hjo]], [[2hqz]], [[2hrs]], [[2okw]], [[2oky]], [[2q57]], [[2due]], [[2duf]], [[2dug]], [[2duh]], [[2dui]], [[2q6p]], [[2hcg]], [[2hfc]], [[2hgd]], [[2hgy]], [[2awj]], [[2awk]], [[2awl]], [[2awm]], [[2g16]], [[2g2s]], [[2g3d]], [[2g5z]], [[2g6e]], [[2ah8]], [[2aha]], [[2fwq]], [[2fzu]], [[2b3p]], [[2b3q]], [[1z1p]], [[1z1q]], [[1yhg]], [[1yhh]], [[1yhi]], [[1yj2]], [[1yjf]], [[1s6z]], [[1q4a]], [[1q4b]], [[1q4c]], [[1q4d]], [[1q4e]], [[1q73]], [[1qyf]], [[1qyo]], [[1qyq]], [[1qst]], [[1qy3]], [[1cv7]], [[1jc0]], [[1jc1]],  [[1jby]], [[1jbz]], [[1kp5]], [[1kyp]], [[1hcj]], [[1h6r]], [[1b9c]], [[1c4f]], [[1emc]], [[1eme]], [[1emf]], [[1emk]], [[1eml]], [[1emm]], [[2emd]], [[2emn]], [[2emo]], [[1emb]], [[1gfl]], [[1ema]], [[2y0g]], [[3gj1]], [[3gj2]], [[3p28]], [[1qxt]] – jGFP (mutant)&amp;lt;br /&amp;gt;&lt;br /&gt;
[[3evp]] – jGFP circular permutation&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2h6v]] – jGFP+imidazole derivative&amp;lt;br /&amp;gt;&lt;br /&gt;
[[1rm9]], [[1rmm]], [[1rmo]], [[1rmp]], [[1rrz]] – jGFP containing fluorotryptophan&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2o24]], [[2o29]], [[2o2b]], [[1w7u]], [[1w7t]], [[1w7s]], [[1emg]] – jGFP (mutant)+imidazole derivative&amp;lt;br /&amp;gt;&lt;br /&gt;
[[1kyr]] – jGFP (mutant)+imidazole derivative+Cu&amp;lt;br /&amp;gt;&lt;br /&gt;
[[1kys]] – jGFP (mutant)+imidazole derivative+Zn&amp;lt;br /&amp;gt;&lt;br /&gt;
[[3ogo]] – jGFP+cGFP nanobody – camel&amp;lt;br /&amp;gt;&lt;br /&gt;
[[3g9a]], [[3k1k]] – jGFP+minimize nanobody – &#039;&#039;Lama pacos&#039;&#039;&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2qle]] – GFP (mutant) – &#039;&#039;Azotobacter vinelandii&#039;&#039;&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2rh7]] – GFP – &#039;&#039;Renilla reniformis&#039;&#039;&amp;lt;br /&amp;gt;&lt;br /&gt;
[[3adf]] – monomeric azami green – &#039;&#039;Galaxea fascicularis&#039;&#039;&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2vzx]] – GFP DENDRA2 – Dendronephthya&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2gw3]] – GFP KAEDE – &#039;&#039;Trachiphyllia geoffroyi&#039;&#039;&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2pox]], [[2gx0]], [[2gx2]], [[2iov]], [[2ie2]] – FP DRONPA – Echinophyllia&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2dd7]] – CpGFP - &#039;&#039;Chiridius poppei&#039;&#039;&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2dd9]] – CpGFP (mutant)&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2c9i]] – saGFP – sea anemone&amp;lt;br /&amp;gt;&lt;br /&gt;
[[1xmz]] – saGFP (mutant)&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2c9j]] – GFP – &#039;&#039;Cerianthus membranaceus&#039;&#039;&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2hpw]] – GFP – &#039;&#039;Clytia gregaria&#039;&#039;&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2g3o]] – PpGFP – &#039;&#039;Pontellina plumata&#039;&#039;&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2g6x]], [[2g6y]] – PpGFP (mutant)&amp;lt;br /&amp;gt;&lt;br /&gt;
[[3lva]], [[3lvc]], [[3lvd]] – GFP (mutant) – &#039;&#039;Aequoarea coerulescens&#039;&#039;&amp;lt;br /&amp;gt;&lt;br /&gt;
&lt;br /&gt;
===Yellow fluorescent protein===&lt;br /&gt;
&lt;br /&gt;
[[3dpw]], [[3dpx]], [[3dpz]], [[3dq1]], [[3dq2]], [[3dq3]], [[3dq4]], [[3dq5]], [[3dq6]], [[3dq7]], [[3dq8]], [[3dq9]], [[3dqa]], [[3dqc]], [[3dqd]], [[3dqe]], [[3dqf]], [[3dqh]], [[3dqi]], [[3dqj]], [[3dqk]], [[3dql]], [[3dqm]], [[3dqn]], [[3dqo]], [[3dqu]], [[1myw]], [[1huy]], [[2yfp]], [[1yfp]] – jGFP (mutant)&amp;lt;br /&amp;gt;&lt;br /&gt;
[[1f09]], [[1f0b]] – jGFP (mutant)+imidazole derivative+I&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2ogr]] – Z-FP - Zoanthus&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2pxs]], [[2pxw]], [[1xa9]], [[1xae]] – Z-FP (mutant)&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2jad]] – jGFP/glutaredoxin&amp;lt;br /&amp;gt;&lt;br /&gt;
&lt;br /&gt;
===Red fluorescent protein===&lt;br /&gt;
&lt;br /&gt;
[[2icr]], [[2ojk]] –  Z-RFP &amp;lt;br /&amp;gt;&lt;br /&gt;
[[2fl1]] – Z-RFP (mutant)&amp;lt;br /&amp;gt;&lt;br /&gt;
[[3bx9]], [[3bxa]], [[3bxb]], [[3bxc]], [[3e5t]], [[3e5w]], [[1uis]], [[3ip2]], [[3pj5]], [[3pj7]], [[3pjb]], [[3pib]] -  EnRFP  – &#039;&#039;Entacmaea quadricolor&#039;&#039;&amp;lt;br /&amp;gt;&lt;br /&gt;
[[3e5v]], [[3rwt]] – EnRFP (mutant)&amp;lt;br /&amp;gt;&lt;br /&gt;
[[1zgo]], [[2vad]], [[2vae]], [[1ggx]] – DiRFP – &#039;&#039;Discosoma&#039;&#039;&amp;lt;br /&amp;gt;&lt;br /&gt;
[[1zgp]], [[1zgq]], [[2h8q]], [[2v4e]], [[1g7k]] – DiRFP (mutant)&amp;lt;br /&amp;gt;&lt;br /&gt;
[[3cfa]] – AsRFP – &#039;&#039;Anemonia sulcata&#039;&#039;&amp;lt;br /&amp;gt;&lt;br /&gt;
[[3nt3]], [[3nt9]] – RFP – artificial gene&amp;lt;br /&amp;gt;&lt;br /&gt;
[[1yzw]] – RFP – &#039;&#039;Heteractis&#039;&#039; &lt;br /&gt;
&lt;br /&gt;
===Cyan fluorescent protein===&lt;br /&gt;
&lt;br /&gt;
[[2wsn]], [[2wso]] - jGFP&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2otb]] – cyan C-FP – Clavularia&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2ote]] - cyan C-FP (mutant)&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2zo6]], [[2zo7]] – cyan FP – &#039;&#039;Fungia concinna&#039;&#039;&amp;lt;br /&amp;gt;&lt;br /&gt;
[[1oxd]], [[1oxe]], [[1oxf]] – cyan FP (mutant) – marker plasmid&amp;lt;br /&amp;gt;&lt;br /&gt;
&lt;br /&gt;
===Blue fluorescent protein===&lt;br /&gt;
&lt;br /&gt;
[[1bfp]] – jGFP (mutant)&lt;br /&gt;
&lt;br /&gt;
===Photoconvertible fluorescent protein===&lt;br /&gt;
&lt;br /&gt;
[[2vvh]], [[2vvi]], [[2vvj]], [[3p8u]] –  LhGFP (mutant) – &#039;&#039;Lobophyllia hemprichii&#039;&#039;&amp;lt;br /&amp;gt;&lt;br /&gt;
[[1zux]] –  LhGFP&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2btj]] -  LhGFP+imidazole derivative&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2ddc]], [[1xss]] –  FfFP – &#039;&#039;Favia favus&#039;&#039;&amp;lt;br /&amp;gt;&lt;br /&gt;
[[2ddd]] -  FfFP (mutant)&amp;lt;br /&amp;gt;&lt;br /&gt;
[[3cff]], [[3cfh]] – AsGFP (mutant)&lt;br /&gt;
&lt;br /&gt;
===Green fluorescent protein chimera===&lt;br /&gt;
&lt;br /&gt;
[[3ai4]] – jGFP/mPolymerase iota ubiquitin binding motif - mouse&amp;lt;br /&amp;gt;&lt;br /&gt;
[[3ai5]] - jGFP/m ubiquitin&amp;lt;br /&amp;gt;&lt;br /&gt;
[[3o77]], [[3o78]], [[3ek4]], [[3ek7]] - jGFP/myosin light chain kinase/calmodulin&amp;lt;br /&amp;gt;&lt;br /&gt;
[[3evr]], [[3evu]], [[3evv]] - jGFP/myosin light chain kinase/calmodulin+Ca&amp;lt;br /&amp;gt;&lt;br /&gt;
[[3ek8]], [[3ekh]], [[3ekj]] - jGFP/myosin light chain kinase/calmodulin (mutant)&amp;lt;br /&amp;gt;&lt;br /&gt;
[[3osq]], [[3osr]] – jGFP/maltose-binding protein&lt;br /&gt;
 &lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
==Reference for this Structure==&lt;br /&gt;
&lt;br /&gt;
Ormo M, Cubitt AB, Kallio K, Gross LA, Tsien RY, Remington SJ.  1996.  Crystal structure of the &#039;&#039;Aequorea victoria&#039;&#039; green fluorescent protein.  Science.  273(5280):1392-1395.  [http://www.sciencemag.org/cgi/content/abstract/273/5280/1392 DOI 10.1126/science.273.5280.1392].&lt;br /&gt;
&lt;br /&gt;
==References==&lt;br /&gt;
&lt;br /&gt;
{{Reflist}}&lt;br /&gt;
&lt;br /&gt;
==Additional Resources==&lt;br /&gt;
*For additional information, see: [[Colored &amp;amp; Bioluminescent Proteins]]&lt;br /&gt;
*[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ema First Glance]&lt;br /&gt;
*PDBsum: [http://www.ebi.ac.uk/pdbsum/1ema 1ema]&lt;br /&gt;
*RCSB PDB [http://www.rcsb.org/pdb/explore.do?structureId=1ema 1ema]&lt;br /&gt;
*[http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ema OCA]&lt;br /&gt;
*UniProt: [http://www.uniprot.org/uniprot/P42212 P42212]&lt;br /&gt;
*Scop: [http://scop.mrc-lmb.cam.ac.uk/scop/data/scop.b.e.gc.b.b.b.html P42212]&lt;br /&gt;
*CATH: [http://www.cathdb.info/domain/1emaA00 1emaA00]&lt;br /&gt;
*Pfam: [http://pfam.sanger.ac.uk/family?acc=PF01353 PF01353]&lt;br /&gt;
*InterPro: [http://www.ebi.ac.uk/interpro/ISearch?query=IPR000786 IPR000786]&lt;br /&gt;
*[http://www.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb42_1.html GFP featured] at the &#039;&#039;&#039;[http://www.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month]&#039;&#039;&#039; series of tutorials by [[User:David_S._Goodsell|David Goodsell]].&lt;br /&gt;
* [http://www.nature.com/nature/journal/v462/n7270/edsumm/e091112-05.html Inside green fluorescent protein] - editor&#039;s summary that accompanied [http://www.nature.com/nature/journal/v462/n7270/covers/ structural detail of GFP chromophore on the cover] of Nature.&lt;br /&gt;
&lt;br /&gt;
[[he:GFP_(Hebrew)]]&lt;br /&gt;
&lt;br /&gt;
[[Category:Topic Page]]&lt;/div&gt;</summary>
		<author><name>Jing Liu</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=Sandbox_CBI&amp;diff=1329520</id>
		<title>Sandbox CBI</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=Sandbox_CBI&amp;diff=1329520"/>
		<updated>2011-12-07T15:36:26Z</updated>

		<summary type="html">&lt;p&gt;Jing Liu: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;!-- &lt;br /&gt;
Please use the &amp;quot;3D&amp;quot; button above this box to insert a Jmol applet (molecule) on this page.&lt;br /&gt;
Or use the four-green-boxes-button to insert scrollable text adjacent&lt;br /&gt;
to a Jmol applet. Check out the other buttons as well! &lt;br /&gt;
--&amp;gt;&lt;br /&gt;
   &lt;br /&gt;
This page is for links to CBI Molecules in Progress (user sandbox pages).&lt;br /&gt;
&lt;br /&gt;
http://proteopedia.org/wiki/index.php/Brittany_deRonde/Sandbox_1&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
http://proteopedia.org/wiki/index.php/Heidi_Hu/Sandbox_1&lt;br /&gt;
&lt;br /&gt;
http://proteopedia.org/wiki/index.php/User:Xuni_Li/Sandbox_1&lt;br /&gt;
&lt;br /&gt;
http://proteopedia.org/wiki/index.php/Gustavo_Elberto_Epalza_Sanchez/Sandbox_1&lt;br /&gt;
&lt;br /&gt;
http://proteopedia.org/wiki/index.php/Scott_Eron/Sandbox1&lt;br /&gt;
&lt;br /&gt;
http://www.proteopedia.org/wiki/index.php/User:Jing_Liu/Sandbox_1&lt;/div&gt;</summary>
		<author><name>Jing Liu</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1329519</id>
		<title>User:Jing Liu/Sandbox 1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Jing_Liu/Sandbox_1&amp;diff=1329519"/>
		<updated>2011-12-07T15:35:56Z</updated>

		<summary type="html">&lt;p&gt;Jing Liu: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;[[Image:intactModelLargeText.jpg|frame|Bacterial chemotaxis receptor]]&lt;br /&gt;
&lt;br /&gt;
This is Jing&#039;s test page.&lt;br /&gt;
&lt;br /&gt;
One of the [[CBI Molecules]] being studied in the  [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].&lt;br /&gt;
&lt;br /&gt;
Many bacteria can &amp;quot;smell&amp;quot; their surroundings and &amp;quot;choose&amp;quot; where to go. They detect molecules such as amino acids or sugars using receptors that bind these molecules and transmit a signal into the cell. This signal controls several proteins which ultimately control the direction of rotation of the motors that rotate the flagella. One direction causes the cell to continue swimming; the other direction causes the cell to tumble. When an attractant molecule binds, the receptor signals: &amp;quot;Things look good, keep swimming!&amp;quot; The opposite signal occurs when bacteria sense a repellant or less attractant molecules: &amp;quot;Time to tumble and try a new swimming direction.&amp;quot;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
A bacterial chemotaxis receptor is an unusually long alpha-helical structure. The attractant molecule (the ligand) binds near the top of this picture and sends a signal across the membrane into the cell to control proteins that bind near the bottom. This is a model of the structure of the receptor based on experimental structures of pieces of related proteins.&lt;br /&gt;
&lt;br /&gt;
{{Clear}}&lt;br /&gt;
&amp;lt;applet load=&#039;1wat&#039; size=&#039;[450,338]&#039; frame=&#039;true&#039; align=&#039;right&#039;&lt;br /&gt;
caption=&#039;Aspartate receptor ligand binding domain (1wat)&#039; scene=&#039;User:Lynmarie_K_Thompson/Sandbox_1/Loadedfrompdb/4&#039;/&amp;gt;&lt;br /&gt;
&lt;br /&gt;
=== Ligand-binding domain ===&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
The spinning protein (&amp;lt;scene name=&#039;User:Lynmarie_K_Thompson/Sandbox_1/Loadedfrompdb/4&#039;&amp;gt;Initial view&amp;lt;/scene&amp;gt;) ) is the ligand binding domain of the aspartate receptor with the aspartate ligand bound (LKT).&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
Molecular Playground banner: A bacterial chemotaxis receptor protein used by bacteria to &amp;quot;smell&amp;quot; their environment.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
{{Clear}}&lt;br /&gt;
&amp;lt;applet load=&#039;2ho9&#039; size=&#039;[450,338]&#039; frame=&#039;true&#039; align=&#039;right&#039;&lt;br /&gt;
caption=&#039;E. coli chemotaxis adaptor protein CheW (2ho9)&#039; scene=&#039;User:Shiela_M._Jones/Sandbox_1/Chew_suppressionmutants/1&#039;/&amp;gt;&lt;br /&gt;
&lt;br /&gt;
=== Chemotaxis adaptor protein CheW ===&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
CheW is a chemotaxis adaptor protein, and part of the tertiary complex formed by the chemotaxis receptor, histidine kinase protein CheA, and CheW.  As an adaptor protein, CheW mediates the interaction between the chemotaxis receptor and CheA, and is necessary for the formation of kinase active complexes.  CheW has been found to bind to the P5 domain of CheA through crystallographic studies.&lt;br /&gt;
&lt;br /&gt;
At right, CheW is shown with suppression mutants (blue)that have been measured to decrease receptor binding and chemotaxis (SMJ).&lt;/div&gt;</summary>
		<author><name>Jing Liu</name></author>
	</entry>
</feed>