Proteopedia - User contributions [en]

Sandbox Reserved 309

2011-04-01T01:56:49Z

Hezzy Cody:

{{Template:Sandbox_Reserved_BCMB307}}

{{STRUCTURE_2cdn|PDB=2cdn|SCENE=}}
__TOC__
=Introduction/General Information=
Adenylate kinase is a phosphotransferase that catalyzes the interconversion reaction of ATP, ADP, and AMP. Phosphotransferases include enzymes that catalyze phosphorylation reactions like the mechanism depicted below. It is part of the nucleotide and nucleoside kinases family. The adenylate kinase family can be classified into two groups: a long variant group, possessing a longer LID domain, and a short variant group where the ''Myobacterium tuberculosis'' bacterium can be found <ref name=Bellinzoni>PMID: 16672241 </ref>. Since the source of this form of adenylate kinase is ''M. tuberculosis'' it is very important in developing treatment for tuberculosis in humans, as it is found to be essential for bacterial survival, and is therefore an excellent target for drugs when treating the disease. <ref name=Bellinzoni>PMID: 16672241 </ref> Since tuberculosis is the leading cause of death from infectious disease worldwide, adenylate kinase is therefore a crucial protein in finding therapeutic tools required for prevention and treatment of this common and deadly disease. <ref name=Miron>PMID:14705932 </ref>
=Structure=
[[Image:LID_and_NMP_region.png]]
Protein of 201 residues with a <scene name='Sandbox_Reserved_309/Ligand/1'>Ligand</scene> consisting of two molecules of ADP (Adenosine-5'-Phosphate) and Magnesium ion. <Structure load=2cdn size='200' frame='true' align='right' caption= 'Adenosine-5'-Diphosphate and Mg' scene='Sandbox_Reserved_309/Ligand/1'/>
==The solution structure==
With no ligand, adenylate kinase is represented by a central CORE domain composed of a 5-stranded parallel beta sheet surrounded by 7 alpha helices, and two periferal domains, LID and NMP <ref name=Miron>PMID:14705932 </ref>, these two binding regions participate in the isolation of the substrates during catalysis and usually undergo significant conformational changes during the reaction <ref name=Bellinzoni>PMID: 16672241 </ref>
==The crystalline structure==
Globular with a central core made by a <scene name='Sandbox_Reserved_309/Beta_parallel_sheet/1'>beta parallel sheet</scene> surrounded by alpha helices, a P-loop motif at the N-terminus that binds ATP, and two regions (LID and NMP).<ref name=Bellinzoni>PMID: 16672241 </ref> The LID region consists of a ten residue loop and is depicted in grey and green in the above image. The NMP-binding region is depicted in orange and dark purple. The overall rearrangement of the NMP binding region is 3.6 angstroms, and 6.4 angstroms in the LID region, indicating that these two regions experience large conformational changes during activation. <ref name=Bellinzoni>PMID: 16672241 </ref>
=Function=
*Involved in nucleotide biosynthesis, which is very important as the intervention point for therapeutic agents.
*Catalyzes the reversible Mg2+ dependent transfer of the terminal phosphate group from ATP to AMP releasing two molecules of ADP or vice versa.
*During the reaction, a molecule of ADP binds to the ATP-binding site, while the NMP-binding site binds either ADP or AMP. The ADP molecule is then phosphorylated in the ATP site and AMP is formed in the NMP site. <ref name=Bellinzoni>PMID: 16672241 </ref>
*LID and NMP binding regions go through a significant conformational change during the catalysis reaction. <ref name=Bellinzoni>PMID: 16672241 </ref>
=Catalytic Mechanism=
The catalytic mechanism facilitated by adenylate kinase is depicted below:

ADP+MgADP↔MgATP+AMP

The geometry of the surrounding amino acids, and the distribution of positive charges of the active sites suggest that there is a direct nucleophilic attack by the oxygen on the donor substrate. Together with the Mg2+ ion, the surrounding side chains are positioned to neutralize the negative transition state and allow the positive polarization required to transfer the phoshporus atom from one of the ADP molecules and therefore create ATP and AMP. <ref name=Bellinzoni>PMID: 16672241 </ref>
=References=
<references/>

Sandbox Reserved 309

2011-04-01T01:54:30Z

Hezzy Cody:

{{Template:Sandbox_Reserved_BCMB307}}

{{STRUCTURE_2cdn|PDB=2cdn|SCENE=}}
__TOC__
=Introduction/General Information=
Adenylate kinase is a phosphotransferase that catalyzes the interconversion reaction of ATP, ADP, and AMP. Phosphotransferases include enzymes that catalyze phosphorylation reactions like the mechanism depicted below. It is part of the nucleotide and nucleoside kinases family. The adenylate kinase family can be classified into two groups: a long variant group, possessing a longer LID domain, and a short variant group where the ''Myobacterium tuberculosis'' bacterium can be found <ref name=Bellinzoni>PMID: 16672241 </ref>. Since the source of this form of adenylate kinase is ''M. tuberculosis'' it is very important in developing treatment for tuberculosis in humans, as it is found to be essential for bacterial survival, and is therefore an excellent target for drugs when treating the disease. <ref name=Bellinzoni>PMID: 16672241 </ref> Since tuberculosis is the leading cause of death from infectious disease worldwide, adenylate kinase is therefore a crucial protein in finding therapeutic tools required for prevention and treatment of this common and deadly disease. <ref name=Miron>PMID:14705932 </ref>
=Structure=
[[Image:LID_and_NMP_region.png]]
Protein of 201 residues with a <scene name='Sandbox_Reserved_309/Ligand/1'>Ligand</scene> consisting of two molecules of ADP (Adenosine-5'-Phosphate) and Magnesium ion. <Structure load=2cdn size='200' frame='true' align='right' caption= 'Adenosine-5'-Diphosphate and Mg' scene='Sandbox_Reserved_309/Ligand/1'/>
==The solution structure==
With no ligand, adenylate kinase is represented by a central CORE domain composed of a 5-stranded parallel beta sheet surrounded by 7 alpha helices, and two periferal domains, LID and NMP <ref name=Miron>PMID:14705932 </ref>, these two binding regions participate in the isolation of the substrates during catalysis and usually undergo significant conformational changes during the reaction <ref name=Bellinzoni>PMID: 16672241 </ref>
==The crystalline structure==
Globular with a central core made by a <scene name='Sandbox_Reserved_309/Beta_parallel_sheet/1'>beta parallel sheet</scene> surrounded by alpha helices, a P-loop motif at the N-terminus that binds ATP, and two regions (LID and NMP).<ref name=Bellinzoni>PMID: 16672241 </ref> The LID region consists of a ten residue loop and is depicted in grey and green in the above image. The NMP-binding region is depicted in orange and dark purple. The overall rearrangement of the NMP binding region is 3.6 angstroms, and 6.4 angstroms in the LID region, indicating that these two regions experience large conformational changes during activation. <ref name=Bellinzoni>PMID: 16672241 </ref>
=Function=
*Involved in nucleotide biosynthesis, which is very important as the intervention point for therapeutic agents.
*Catalyzes the reversible Mg2+ dependent transfer of the terminal phosphate group from ATP to AMP releasing two molecules of ADP.
*During the reaction, a molecule of ADP binds to the ATP-binding site, while the NMP-binding site binds either ADP or AMP. The ADP molecule is then phosphorylated in the ATP site and AMP is formed in the NMP site. <ref name=Bellinzoni>PMID: 16672241 </ref>
*LID and NMP binding regions go through a significant conformational change during the catalysis reaction. <ref name=Bellinzoni>PMID: 16672241 </ref>
=Catalytic Mechanism=
The catalytic mechanism facilitated by adenylate kinase is depicted below:

ADP+MgADP↔MgATP+AMP

The geometry of the surrounding amino acids, and the distribution of positive charges of the active sites suggest that there is a direct nucleophilic attack by the oxygen on the donor substrate. Together with the Mg2+ ion, the surrounding side chains are positioned to neutralize the negative transition state and allow the positive polarization required to transfer the phoshporus atom from one of the ADP molecules and therefore create ATP and AMP. <ref name=Bellinzoni>PMID: 16672241 </ref>
=References=
<references/>

Sandbox Reserved 309

2011-04-01T01:49:57Z

Hezzy Cody:

{{Template:Sandbox_Reserved_BCMB307}}

{{STRUCTURE_2cdn|PDB=2cdn|SCENE=}}
__TOC__
=Introduction/General Information=
Adenylate kinase is a phosphotransferase that catalyzes the interconversion reaction of ATP, ADP, and AMP. Phosphotransferases include enzymes that catalyze phosphorylation reactions like the mechanism depicted below. It is part of the nucleotide and nucleoside kinases family. The adenylate kinase family can be classified into two groups: a long variant group, possessing a longer LID domain, and a short variant group where the ''Myobacterium tuberculosis'' bacterium can be found <ref name=Bellinzoni>PMID: 16672241 </ref>. Since the source of this form of adenylate kinase is ''M. tuberculosis'' it is very important in developing treatment for tuberculosis in humans, as it is found to be essential for bacterial survival, and is therefore an excellent target for drugs when treating the disease. <ref name=Bellinzoni>PMID: 16672241 </ref> Since tuberculosis is the leading cause of death from infectious disease worldwide, adenylate kinase is therefore a crucial protein in finding therapeutic tools required for prevention and treatment of this common and deadly disease. <ref name=Miron>PMID:14705932 </ref>
=Structure=
[[Image:LID_and_NMP_region.png]]
Protein of 201 residues with a <scene name='Sandbox_Reserved_309/Ligand/1'>Ligand</scene> consisting of two molecules of ADP (Adenosine-5'-Phosphate) and Magnesium ion. <Structure load=2cdn size='200' frame='true' align='right' caption= 'Adenosine-5'-Diphosphate and Mg' scene='Sandbox_Reserved_309/Ligand/1'/>
==The solution structure==
With no ligand, adenylate kinase is represented by a central CORE domain composed of a 5-stranded parallel beta sheet surrounded by 7 alpha helices, and two periferal domains, LID and NMP <ref name=Miron>PMID:14705932 </ref>, these two binding regions participate in the isolation of the substrates during catalysis and usually undergo significant conformational changes during the reaction <ref name=Bellinzoni>PMID: 16672241 </ref>
==The crystalline structure==
Globular with a central core made by a <scene name='Sandbox_Reserved_309/Beta_parallel_sheet/1'>beta parallel sheet</scene> surrounded by alpha helices, a P-loop motif at the N-terminus that binds ATP, and two regions (LID and NMP).<ref name=Bellinzoni>PMID: 16672241 </ref> The LID region consists of a ten residue loop and is depicted in grey and green in the above image. The NMP-binding region is depicted in orange and dark purple. The overall rearrangement of the NMP binding region is 3.6 angstroms, and 6.4 angstroms in the LID region, indicating that these two regions experience large conformational changes during activation. <ref name=Bellinzoni>PMID: 16672241 </ref>
=Function=
*Involved in nucleotide biosynthesis, which is very important as the intervention point for therapeutic agents.
*Catalyzes the reversible Mg2+ dependent transfer of the terminal phosphate group from ATP to AMP releasing two molecules of ADP.
*During the reaction, a molecule of ADP binds to the ATP-binding site, while the NMP-binding site binds either ADP or AMP. The ADP molecule is then phosphorylated in the ATP site and AMP is formed in the NMP site. <ref name=Bellinzoni>PMID: 16672241 </ref>
*LID and NMP binding regions go through a significant conformational change during the catalysis reaction depicted below. <ref name=Bellinzoni>PMID: 16672241 </ref>
=Catalytic Mechanism=
The catalytic mechanism facilitated by adenylate kinase is depicted below:

ADP+MgADP↔MgATP+AMP

The geometry of the surrounding amino acids, and the distribution of positive charges of the active sites suggest that there is a direct nucleophilic attack by the oxygen on the donor substrate. Together with the Mg2+ ion, the surrounding side chains are positioned to neutralize the negative transition state and allow the positive polarization required to transfer the phoshporus atom from one of the ADP molecules and therefore create ATP and AMP. <ref name=Bellinzoni>PMID: 16672241 </ref>
=References=
<references/>

Sandbox Reserved 309

2011-04-01T01:48:44Z

Hezzy Cody:

{{Template:Sandbox_Reserved_BCMB307}}

{{STRUCTURE_2cdn|PDB=2cdn|SCENE=}}
__TOC__
=Introduction/General Information=
Adenylate kinase is a phosphotransferase that catalyzes the interconversion reaction of ATP, ADP, and AMP. Phosphotransferases include enzymes that catalyze phosphorylation reactions like the mechanism depicted below. It is part of the nucleotide and nucleoside kinases family. The adenylate kinase family can be classified into two groups: a long variant group, possessing a longer LID domain, and a short variant group where the ''Myobacterium tuberculosis'' bacterium can be found <ref name=Bellinzoni>PMID: 16672241 </ref>. Since the source of this form of adenylate kinase is ''M. tuberculosis'' it is very important in developing treatment for tuberculosis in humans, as it is found to be essential for bacterial survival, and is therefore an excellent target for drugs when treating the disease. <ref name=Bellinzoni>PMID: 16672241 </ref> Since tuberculosis is the leading cause of death from infectious disease worldwide, adenylate kinase is therefore a crucial protein in finding therapeutic tools required for prevention and treatment of this common and deadly disease. <ref name=Miron>PMID:14705932 </ref>
=Structure=
[[Image:LID_and_NMP_region.png]]
Protein of 201 residues with a <scene name='Sandbox_Reserved_309/Ligand/1'>Ligand</scene> consisting of two molecules of ADP (Adenosine-5'-Phosphate) and Magnesium ion. <Structure load=2cdn size='200' frame='true' align='right' caption= 'Adenosine-5'-Diphosphate and Mg' scene='Sandbox_Reserved_309/Ligand/1'/>
==The solution structure==
With no ligand, is represented by a central CORE domain composed of a 5-stranded parallel beta sheet surrounded by 7 alpha helices, and two periferal domains, LID and NMP <ref name=Miron>PMID:14705932 </ref>, these two binding regions participate in the isolation of the substrates during catalysis and usually undergo significant conformational changes during the reaction <ref name=Bellinzoni>PMID: 16672241 </ref>
==The crystalline structure==
Globular with a central core made by a <scene name='Sandbox_Reserved_309/Beta_parallel_sheet/1'>beta parallel sheet</scene> surrounded by alpha helices, a P-loop motif at the N-terminus that binds ATP, and two regions (LID and NMP).<ref name=Bellinzoni>PMID: 16672241 </ref> The LID region consists of a ten residue loop and is depicted in grey and green in the above image. The NMP-binding region is depicted in orange and dark purple. The overall rearrangement of the NMP binding region is 3.6 angstroms, and 6.4 angstroms in the LID region, indicating that these two regions experience large conformational changes during activation. <ref name=Bellinzoni>PMID: 16672241 </ref>
=Function=
*Involved in nucleotide biosynthesis, which is very important as the intervention point for therapeutic agents.
*Catalyzes the reversible Mg2+ dependent transfer of the terminal phosphate group from ATP to AMP releasing two molecules of ADP.
*During the reaction, a molecule of ADP binds to the ATP-binding site, while the NMP-binding site binds either ADP or AMP. The ADP molecule is then phosphorylated in the ATP site and AMP is formed in the NMP site. <ref name=Bellinzoni>PMID: 16672241 </ref>
*LID and NMP binding regions go through a significant conformational change during the catalysis reaction depicted below. <ref name=Bellinzoni>PMID: 16672241 </ref>
=Catalytic Mechanism=
The catalytic mechanism facilitated by adenylate kinase is depicted below:

ADP+MgADP↔MgATP+AMP

The geometry of the surrounding amino acids, and the distribution of positive charges of the active sites suggest that there is a direct nucleophilic attack by the oxygen on the donor substrate. Together with the Mg2+ ion, the surrounding side chains are positioned to neutralize the negative transition state and allow the positive polarization required to transfer the phoshporus atom from one of the ADP molecules and therefore create ATP and AMP. <ref name=Bellinzoni>PMID: 16672241 </ref>
=References=
<references/>

Sandbox Reserved 309

2011-04-01T01:48:02Z

Hezzy Cody:

{{Template:Sandbox_Reserved_BCMB307}}

{{STRUCTURE_2cdn|PDB=2cdn|SCENE=}}
__TOC__
=Introduction/General Information=
Adenylate kinase is a phosphotransferase that catalyzes the interconversion reaction of ATP, ADP, and AMP. Phosphotransferases include enzymes that catalyze phosphorylation reactions like the mechanism depicted below. It is part of the nucleotide and nucleoside kinases family. The adenylate kinase family can be classified into two groups: a long variant group, possessing a longer LID domain, and a short variant group where the ''Myobacterium tuberculosis'' bacterium can be found <ref name=Bellinzoni>PMID: 16672241 </ref>. Since the source of this form of adenylate kinase is ''M. tuberculosis'' it is very important in developing treatment for tuberculosis in humans, as it is found to be essential for bacterial survival, and is therefore an excellent target for drugs when treating the disease. <ref name=Bellinzoni>PMID: 16672241 </ref> Since tuberculosis is the leading cause of death from infectious disease worldwide, adenylate kinase is therefore a crucial protein in finding therapeutic tools required for prevention and treatment of this common and deadly disease.
=Structure=
[[Image:LID_and_NMP_region.png]]
Protein of 201 residues with a <scene name='Sandbox_Reserved_309/Ligand/1'>Ligand</scene> consisting of two molecules of ADP (Adenosine-5'-Phosphate) and Magnesium ion. <Structure load=2cdn size='200' frame='true' align='right' caption= 'Adenosine-5'-Diphosphate and Mg' scene='Sandbox_Reserved_309/Ligand/1'/>
==The solution structure==
With no ligand, is represented by a central CORE domain composed of a 5-stranded parallel beta sheet surrounded by 7 alpha helices, and two periferal domains, LID and NMP <ref name=Miron>PMID:14705932 </ref>, these two binding regions participate in the isolation of the substrates during catalysis and usually undergo significant conformational changes during the reaction <ref name=Bellinzoni>PMID: 16672241 </ref>
==The crystalline structure==
Globular with a central core made by a <scene name='Sandbox_Reserved_309/Beta_parallel_sheet/1'>beta parallel sheet</scene> surrounded by alpha helices, a P-loop motif at the N-terminus that binds ATP, and two regions (LID and NMP).<ref name=Bellinzoni>PMID: 16672241 </ref> The LID region consists of a ten residue loop and is depicted in grey and green in the above image. The NMP-binding region is depicted in orange and dark purple. The overall rearrangement of the NMP binding region is 3.6 angstroms, and 6.4 angstroms in the LID region, indicating that these two regions experience large conformational changes during activation. <ref name=Bellinzoni>PMID: 16672241 </ref>
=Function=
*Involved in nucleotide biosynthesis, which is very important as the intervention point for therapeutic agents.
*Catalyzes the reversible Mg2+ dependent transfer of the terminal phosphate group from ATP to AMP releasing two molecules of ADP.
*During the reaction, a molecule of ADP binds to the ATP-binding site, while the NMP-binding site binds either ADP or AMP. The ADP molecule is then phosphorylated in the ATP site and AMP is formed in the NMP site. <ref name=Bellinzoni>PMID: 16672241 </ref>
*LID and NMP binding regions go through a significant conformational change during the catalysis reaction depicted below. <ref name=Bellinzoni>PMID: 16672241 </ref>
=Catalytic Mechanism=
The catalytic mechanism facilitated by adenylate kinase is depicted below:

ADP+MgADP↔MgATP+AMP

The geometry of the surrounding amino acids, and the distribution of positive charges of the active sites suggest that there is a direct nucleophilic attack by the oxygen on the donor substrate. Together with the Mg2+ ion, the surrounding side chains are positioned to neutralize the negative transition state and allow the positive polarization required to transfer the phoshporus atom from one of the ADP molecules and therefore create ATP and AMP. <ref name=Bellinzoni>PMID: 16672241 </ref>
=References=
<references/>

Sandbox Reserved 309

2011-04-01T01:40:01Z

Hezzy Cody:

{{Template:Sandbox_Reserved_BCMB307}}

{{STRUCTURE_2cdn|PDB=2cdn|SCENE=}}
__TOC__
=Introduction/General Information=
Adenylate kinase is a phosphotransferase that catalyzes the interconversion reaction of ATP, ADP, and AMP. Phosphotransferases include enzymes that catalyze phosphorylation reactions like the mechanism depicted below. It is part of the nucleotide and nucleoside kinases family. The adenylate kinase family can be classified into two groups: a long variant group, possessing a longer LID domain, and a short variant group where the ''Myobacterium tuberculosis'' bacterium can be found <ref name=Bellinzoni>PMID: 16672241 </ref>. Since the source of this form of adenylate kinase is ''M. tuberculosis'' it is very important in developing treatment for tuberculosis in humans, as it is found to be essential for bacterial survival, and is therefore an excellent target for drugs when treating the disease. <ref name=Bellinzoni>PMID: 16672241 </ref>
=Structure=
[[Image:LID_and_NMP_region.png]]
Protein of 201 residues with a <scene name='Sandbox_Reserved_309/Ligand/1'>Ligand</scene> consisting of two molecules of ADP (Adenosine-5'-Phosphate) and Magnesium ion. <Structure load=2cdn size='200' frame='true' align='right' caption= 'Adenosine-5'-Diphosphate and Mg' scene='Sandbox_Reserved_309/Ligand/1'/>
==The solution structure==
With no ligand, is represented by a central CORE domain composed of a 5-stranded parallel beta sheet surrounded by 7 alpha helices, and two periferal domains, LID and NMP <ref name=Miron>PMID:14705932 </ref>, these two binding regions participate in the isolation of the substrates during catalysis and usually undergo significant conformational changes during the reaction <ref name=Bellinzoni>PMID: 16672241 </ref>
==The crystalline structure==
Globular with a central core made by a <scene name='Sandbox_Reserved_309/Beta_parallel_sheet/1'>beta parallel sheet</scene> surrounded by alpha helices, a P-loop motif at the N-terminus that binds ATP, and two regions (LID and NMP).<ref name=Bellinzoni>PMID: 16672241 </ref> The LID region consists of a ten residue loop and is depicted in grey and green in the above image. The NMP-binding region is depicted in orange and dark purple. The overall rearrangement of the NMP binding region is 3.6 angstroms, and 6.4 angstroms in the LID region, indicating that these two regions experience large conformational changes during activation. <ref name=Bellinzoni>PMID: 16672241 </ref>
=Function=
*Involved in nucleotide biosynthesis, which is very important as the intervention point for therapeutic agents.
*Catalyzes the reversible Mg2+ dependent transfer of the terminal phosphate group from ATP to AMP releasing two molecules of ADP.
*During the reaction, a molecule of ADP binds to the ATP-binding site, while the NMP-binding site binds either ADP or AMP. The ADP molecule is then phosphorylated in the ATP site and AMP is formed in the NMP site. <ref name=Bellinzoni>PMID: 16672241 </ref>
*LID and NMP binding regions go through a significant conformational change during the catalysis reaction depicted below. <ref name=Bellinzoni>PMID: 16672241 </ref>
=Catalytic Mechanism=
The catalytic mechanism facilitated by adenylate kinase is depicted below:

ADP+MgADP↔MgATP+AMP

The geometry of the surrounding amino acids, and the distribution of positive charges of the active sites suggest that there is a direct nucleophilic attack by the oxygen on the donor substrate. Together with the Mg2+ ion, the surrounding side chains are positioned to neutralize the negative transition state and allow the positive polarization required to transfer the phoshporus atom from one of the ADP molecules and therefore create ATP and AMP. <ref name=Bellinzoni>PMID: 16672241 </ref>
=References=
<references/>

Sandbox Reserved 309

2011-04-01T01:25:54Z

Hezzy Cody:

{{Template:Sandbox_Reserved_BCMB307}}

{{STRUCTURE_2cdn|PDB=2cdn|SCENE=}}
__TOC__
=Introduction/General Information=
Adenylate kinase is a phosphotransferase that catalyzes the interconversion reaction of ATP, ADP, and AMP. Phosphotransferases include enzymes that catalyze phosphorylation reactions like the mechanism depicted below. It is part of the nucleotide and nucleoside kinases family. The adenylate kinase family can be classified into two groups: a long variant group, possessing a longer LID domain, and a short variant group where the ''Myobacterium tuberculosis'' bacterium can be found <ref name=Bellinzoni>PMID: 16672241 </ref>. Since the source of this form of adenylate kinase is ''M. tuberculosis'' it is very important in developing treatment for tuberculosis in humans, as it is found to be essential for bacterial survival, and is therefore an excellent target for drugs when treating the disease. <ref name=Bellinzoni>PMID: 16672241 </ref>
=Structure=
[[Image:LID_and_NMP_region.png]]
Protein of 201 residues with a <scene name='Sandbox_Reserved_309/Ligand/1'>Ligand</scene> consisting of two molecules of ADP (Adenosine-5'-Phosphate) and Magnesium ion. <Structure load=2cdn size='200' frame='true' align='right' caption= 'Adenosine-5'-Diphosphate and Mg' scene='Sandbox_Reserved_309/Ligand/1'/>
==The solution structure==
With no ligand, is represented by a central CORE domain composed of a 5-stranded parallel beta sheet surrounded by 7 alpha helices, and two periferal domains, LID and NMP <ref name=Miron>PMID:14705932 </ref>, these two binding regions participate in the isolation of the substrates during catalysis and usually undergo significant conformational changes during the reaction <ref name=Bellinzoni>PMID: 16672241 </ref>
==The crystalline structure==
Globular with a central core made by a <scene name='Sandbox_Reserved_309/Beta_parallel_sheet/1'>beta parallel sheet</scene> surrounded by alpha helices, a P-loop motif at the N-terminus that binds ATP, and two regions (LID and NMP).<ref name=Bellinzoni>PMID: 16672241 </ref> The LID region consists of a ten residue loop and is depicted in grey and green in the above image. The NMP-binding region is depicted in orange and dark purple. The overall rearrangement of the NMP binding region is 3.6 angstroms, and 6.4 angstroms in the LID region, indicating that these two regions experience large conformational changes during activation. <ref name=Bellinzoni>PMID: 16672241 </ref>
=Function=
*Involved in nucleotide biosynthesis, which is very important as the intervention point for therapeutic agents.
*Catalyzes the reversible Mg2+ dependent transfer of the terminal phosphate group from ATP to AMP releasing two molecules of ADP.
*During the reaction, a molecule of ADP binds to the ATP-binding site, while the NMP-binding site binds either ADP or AMP. The ADP molecule is then phosphorylated in the ATP site and AMP is formed in the NMP site. <ref name=Bellinzoni>PMID: 16672241 </ref>
*LID and NMP binding regions go through a significant conformational change during the catalysis reaction depicted below. <ref name=Bellinzoni>PMID: 16672241 </ref>
=Catalytic Mechanism=
ADP+MgADP↔MgATP+AMP
=References=
<references/>

Sandbox Reserved 309

2011-04-01T01:20:45Z

Hezzy Cody:

{{Template:Sandbox_Reserved_BCMB307}}

{{STRUCTURE_2cdn|PDB=2cdn|SCENE=}}
__TOC__
=Introduction/General Information=
Adenylate kinase is a phosphotransferase that catalyzes the interconversion reaction of ATP, ADP, and AMP. Phosphotransferases include enzymes that catalyze phosphorylation reactions like the mechanism depicted below. It is part of the nucleotide and nucleoside kinases family. The adenylate kinase family can be classified into two groups: a long variant group, possessing a longer LID domain, and a short variant group where the ''Myobacterium tuberculosis'' bacterium can be found <ref name=Bellinzoni>PMID: 16672241 </ref>. Since the source of this form of adenylate kinase is ''M. tuberculosis'' it is very important in developing treatment for tuberculosis in humans, as it is found to be essential for bacterial survival, and is therefore an excellent target for drugs when treating the disease. <ref name=Bellinzoni>PMID: 16672241 </ref>
=Structure=
[[Image:LID_and_NMP_region.png]]
Protein of 201 residues with a <scene name='Sandbox_Reserved_309/Ligand/1'>Ligand</scene> consisting of two molecules of ADP (Adenosine-5'-Phosphate) and Magnesium ion. <Structure load=2cdn size='200' frame='true' align='right' caption= 'Adenosine-5'-Diphosphate and Mg' scene='Sandbox_Reserved_309/Ligand/1'/>
==The solution structure==
With no ligand, is represented by a central CORE domain composed of a 5-stranded parallel beta sheet surrounded by 7 alpha helices, and two periferal domains, LID and NMP <ref name=Miron>PMID:14705932 </ref>, these two binding regions participate in the isolation of the substrates during catalysis and usually undergo significant conformational changes during the reaction <ref name=Bellinzoni>PMID: 16672241 </ref>
==The crystalline structure==
Globular with a central core made by a <scene name='Sandbox_Reserved_309/Beta_parallel_sheet/1'>beta parallel sheet</scene> surrounded by alpha helices, a P-loop motif at the N-terminus that binds ATP, and two regions (LID and NMP).<ref name=Bellinzoni>PMID: 16672241 </ref> The LID region consists of a ten residue loop and is depicted in grey and green in the above image. The NMP-binding region is depicted in orange and dark purple. The overall rearrangement of the NMP binding region is 3.6 angstroms, and 6.4 angstroms in the LID region, indicating that these two regions experience large conformational changes during activation. <ref name=Bellinzoni>PMID: 16672241 </ref>
=Function=
*Involved in nucleotide biosynthesis, which is very important as the intervention point for therapeutic agents.
*Catalyzes the reversible Mg2+ dependent transfer of the terminal phosphate group from ATP to AMP releasing two molecules of ADP.
*LID and NMP binding regions go through a significant conformational change during the catalysis reaction depicted below. <ref name=Bellinzoni>PMID: 16672241 </ref>
=Catalytic Mechanism=
ADP+MgADP↔MgATP+AMP
=References=
<references/>

File:LID and NMP region.png

2011-04-01T01:13:37Z

Hezzy Cody: Picture developed using Swiss PDB

== Summary ==
Picture developed using Swiss PDB
== Licensing ==
{{self|cc-by-3.0}}

Sandbox Reserved 309

2011-04-01T01:09:14Z

Hezzy Cody:

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2011-04-01T01:03:01Z

Hezzy Cody:

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2011-04-01T01:02:23Z

Hezzy Cody:

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2011-04-01T00:51:51Z

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2011-04-01T00:45:54Z

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2011-04-01T00:30:20Z

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2011-03-31T09:08:21Z

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2011-03-31T09:06:22Z

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2011-03-31T08:58:38Z

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2011-03-18T02:19:35Z

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2011-03-18T02:16:17Z

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{{Template:Sandbox_Reserved_BCMB307}}

__TOC__
{{STRUCTURE_2cdn|PDB=2cdn|SCENE=}}
=Introduction/General Information=
Adenylate kinase is a phosphotransferase that catalyzes the interconversion reaction of ATP, ADP, and AMP. It is part of the nucleotide and nucleoside kinases family. Its source is the Myobacterium tuberculosis bacterium. Since Adenylate Kinase is found to be essential for bacterial survival, it is targeted by drugs when treating the disease. <ref name=Bellinzoni>PMID: 16672241 </ref>
=Structure=
Protein of 201 residues with a <scene name='Sandbox_Reserved_309/Ligand/1'>Ligand</scene>
consisting of two molecules of ADP (Adenosine-5'-Phosphate) and Magnesium ion.
==The solution structure==
With no ligand, is represented by a central CORE domain composed of a 5-stranded parallel beta sheet surrounded by 7 alpha helices, and two periferal domains, LID and NMP <ref name=Miron>PMID:14705932 </ref>
==The crystalline structure==
Globular with a central core made by beta parallel sheet surrounded by alpha helices, a P-loop motif at the N-terminus that binds ATP, and two regions (LID and NMP). <ref name=Bellinzoni>PMID: 16672241 </ref>
=Function=
Involved in nucleotide biosynthesis. Catalyzes the reversible Mg2+ dependent transfer of the terminal phosphate group from ATP to AMP releasing two molecules of ADP. LID and NMP binding regions go through a significant conformational change during the catalysis reaction depicted below. <ref name=Bellinzoni>PMID: 16672241 </ref>
=Catalytic Mechanism=
ADP+MgADP↔MgATP+AMP
*bullet
**subbullet
*bullet2
<Structure load=2cdn size='200' frame='true' align='left' caption= 'Adenosine-5'-Diphosphate and Mg' scene='Sandbox_Reserved_309/Ligand/1'/>
α
=references=
<references/>

Sandbox Reserved 309

2011-03-18T02:13:45Z

Hezzy Cody:

{{Template:Sandbox_Reserved_BCMB307}}

__TOC__
=Introduction/General Information=
Adenylate kinase is a phosphotransferase that catalyzes the interconversion reaction of ATP, ADP, and AMP. It is part of the nucleotide and nucleoside kinases family. Its source is the Myobacterium tuberculosis bacterium. Since Adenylate Kinase is found to be essential for bacterial survival, it is targeted by drugs when treating the disease. <ref name=Bellinzoni>PMID: 16672241 </ref>

=Structure=
Protein of 201 residues with a ligand consisting of two molecules of ADP (Adenosine-5'-Phosphate) and Magnesium ion.<scene name='Sandbox_Reserved_309/Ligand/1'>Ligand</scene>
==The solution structure==
With no ligand, is represented by a central CORE domain composed of a 5-stranded parallel beta sheet surrounded by 7 alpha helices, and two periferal domains, LID and NMP <ref name=Miron>PMID:14705932 </ref>
==The crystalline structure==
Globular with a central core made by beta parallel sheet surrounded by alpha helices, a P-loop motif at the N-terminus that binds ATP, and two regions (LID and NMP). <ref name=Bellinzoni>PMID: 16672241 </ref>
{{STRUCTURE_2cdn|PDB=2cdn|SCENE=}}
=Function=
Involved in nucleotide biosynthesis. Catalyzes the reversible Mg2+ dependent transfer of the terminal phosphate group from ATP to AMP releasing two molecules of ADP. LID and NMP binding regions go through a significant conformational change during the catalysis reaction depicted below. <ref name=Bellinzoni>PMID: 16672241 </ref>

=Catalytic Mechanism=
ADP+MgADP↔MgATP+AMP
*bullet
**subbullet
*bullet2
<Structure load=2cdn size='200' frame='true' align='left' caption= 'Adenosine-5'-Diphosphate and Mg' scene='Sandbox_Reserved_309/Ligand/1'/>
α
=references=
<references/>

Sandbox Reserved 309

2011-03-18T01:50:01Z

Hezzy Cody:

{{Template:Sandbox_Reserved_BCMB307}}

__TOC__
=Introduction/General Information=
Adenylate kinase is a phosphotransferase that catalyzes the interconversion reaction of ATP, ADP, and AMP. It is part of the nucleotide and nucleoside kinases family. Its source is the Myobacterium tuberculosis bacterium. Since Adenylate Kinase is found to be essential for bacterial survival, it is targeted by drugs when treating the disease.
=Structure==
Protein of 201 residues with a ligand consisting of two molecules of ADP (Adenosine-5'-Phosphate) and Magnesium ion.
<Structure load=2cdn size='200' frame='true' align='left' caption= 'Adenosine-5'-Diphosphate and Mg' scene='Sandbox_Reserved_309/Ligand/1'/>
==The solution structure==
With no ligand, is represented by a central CORE domain composed of a 5-stranded parallel beta sheet surrounded by 7 alpha helices, and two periferal domains, LID and NMP <ref name=Miron>PMID:14705932 </ref>
==The crystalline structure==
Globular with a central core made by beta parallel sheet surrounded by alpha helices, a P-loop motif at the N-terminus that binds ATP, and two regions (LID and NMP).
{{STRUCTURE_2cdn|PDB=2cdn|SCENE=}}
=Function=
Involved in nucleotide biosynthesis. Catalyzes the reversible Mg2+ dependent transfer of the terminal phosphate group from ATP to AMP releasing two molecules of ADP. LID and NMP binding regions go through a significant conformational change during the catalysis reaction depicted below.
=Catalytic Mechanism=
ADP+MgADP↔MgATP+AMP
<scene name='Sandbox_Reserved_309/Ligand/1'>Ligand</scene>
*bullet
**subbullet
*bullet2
α
=references=
<references/>

Sandbox Reserved 309

2011-03-17T10:48:42Z

Hezzy Cody:

{{Template:Sandbox_Reserved_BCMB307}}

=Introduction=
__TOC__
=section 1=
{{STRUCTURE_2cdn|PDB=2cdn|SCENE=}}
==section 1.1==
==section 1.2==
===subsection 1.21===
=section2=
<scene name='Sandbox_Reserved_309/Ligand/1'>Ligand</scene>
*bullet
**subbullet
*bullet2
<Structure load=2cdn size='200' frame='true' align='left' caption= 'Adenosine-5'-Diphosphate and Mg' scene='Sandbox_Reserved_309/Ligand/1'/>
α
<ref name=lastname1stauthor>PMID:number </ref>
=references=
<references/>
hi my name is <br/> Hezzy