1ku3: Difference between revisions

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[[Image:1ku3.gif|left|200px]]<br /><applet load="1ku3" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1ku3.gif|left|200px]]<br /><applet load="1ku3" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1ku3, resolution 1.8Å" />

'''Crystal Structure of Thermus aquaticus RNA Polymerase Sigma Subunit Fragment, Region 4'''<br />

==Overview==

The sigma subunit is the key regulator of bacterial transcription., Proteolysis of Thermus aquaticus sigma(A), which occurred in situ during, crystallization, reveals three domains, sigma(2), sigma(3), and sigma(4), connected by flexible linkers. Crystal structures of each domain were, determined, as well as of sigma(4) complexed with -35 element DNA. Exposed, surfaces of each domain are important for RNA polymerase binding., Universally conserved residues important for -10 element recognition and, melting lie on one face of sigma(2), while residues important for extended, -10 recognition lie on sigma(3). Genetic studies correctly predicted that, a helix-turn-helix motif in sigma(4) recognizes the -35 element but not, the details of the protein-DNA interactions. Positive control mutants in, sigma(4) cluster in two regions, positioned to interact with activators, bound just upstream or downstream of the -35 element.

The sigma subunit is the key regulator of bacterial transcription. Proteolysis of Thermus aquaticus sigma(A), which occurred in situ during crystallization, reveals three domains, sigma(2), sigma(3), and sigma(4), connected by flexible linkers. Crystal structures of each domain were determined, as well as of sigma(4) complexed with -35 element DNA. Exposed surfaces of each domain are important for RNA polymerase binding. Universally conserved residues important for -10 element recognition and melting lie on one face of sigma(2), while residues important for extended -10 recognition lie on sigma(3). Genetic studies correctly predicted that a helix-turn-helix motif in sigma(4) recognizes the -35 element but not the details of the protein-DNA interactions. Positive control mutants in sigma(4) cluster in two regions, positioned to interact with activators bound just upstream or downstream of the -35 element.

==About this Structure==

1KU3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1KU3 OCA].

1KU3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KU3 OCA].

==Reference==

Line 13:

[[Category: Single protein]]

[[Category: Thermus aquaticus]]

[[Category: Campbell, E.A.]]

[[Category: Campbell, E A.]]

[[Category: Chlenov, M.]]

[[Category: Darst, S.A.]]

[[Category: Darst, S A.]]

[[Category: Muzzin, O.]]

[[Category: Olson, C.A.]]

[[Category: Olson, C A.]]

[[Category: Sun, J.L.]]

[[Category: Sun, J L.]]

[[Category: Trester-Zedlitz, M.L.]]

[[Category: Trester-Zedlitz, M L.]]

[[Category: Weinman, O.]]

[[Category: helix-turn-helix]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Sun Nov 25 01~~:57:~~12 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:37:56 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1ku3.gif|left|200px]]<br /><applet load="1ku3" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1ku3.gif|left|200px]]<br /><applet load="1ku3" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1ku3, resolution 1.8&Aring;" />
 '''Crystal Structure of Thermus aquaticus RNA Polymerase Sigma Subunit Fragment, Region 4'''<br />
 ==Overview==
-The sigma subunit is the key regulator of bacterial transcription., Proteolysis of Thermus aquaticus sigma(A), which occurred in situ during, crystallization, reveals three domains, sigma(2), sigma(3), and sigma(4), connected by flexible linkers. Crystal structures of each domain were, determined, as well as of sigma(4) complexed with -35 element DNA. Exposed, surfaces of each domain are important for RNA polymerase binding., Universally conserved residues important for -10 element recognition and, melting lie on one face of sigma(2), while residues important for extended, -10 recognition lie on sigma(3). Genetic studies correctly predicted that, a helix-turn-helix motif in sigma(4) recognizes the -35 element but not, the details of the protein-DNA interactions. Positive control mutants in, sigma(4) cluster in two regions, positioned to interact with activators, bound just upstream or downstream of the -35 element.
+The sigma subunit is the key regulator of bacterial transcription. Proteolysis of Thermus aquaticus sigma(A), which occurred in situ during crystallization, reveals three domains, sigma(2), sigma(3), and sigma(4), connected by flexible linkers. Crystal structures of each domain were determined, as well as of sigma(4) complexed with -35 element DNA. Exposed surfaces of each domain are important for RNA polymerase binding. Universally conserved residues important for -10 element recognition and melting lie on one face of sigma(2), while residues important for extended -10 recognition lie on sigma(3). Genetic studies correctly predicted that a helix-turn-helix motif in sigma(4) recognizes the -35 element but not the details of the protein-DNA interactions. Positive control mutants in sigma(4) cluster in two regions, positioned to interact with activators bound just upstream or downstream of the -35 element.
 ==About this Structure==
-KU3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KU3 OCA].
+KU3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KU3 OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Single protein]]
 [[Category: Thermus aquaticus]]
-[[Category: Campbell, E.A.]]
+[[Category: Campbell, E A.]]
 [[Category: Chlenov, M.]]
-[[Category: Darst, S.A.]]
+[[Category: Darst, S A.]]
 [[Category: Muzzin, O.]]
-[[Category: Olson, C.A.]]
+[[Category: Olson, C A.]]
-[[Category: Sun, J.L.]]
+[[Category: Sun, J L.]]
-[[Category: Trester-Zedlitz, M.L.]]
+[[Category: Trester-Zedlitz, M L.]]
 [[Category: Weinman, O.]]
 [[Category: helix-turn-helix]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 01:57:12 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:37:56 2008''