1i6a: Difference between revisions

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[[Image:1i6a.jpg|left|200px]]<br /><applet load="1i6a" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1i6a.jpg|left|200px]]<br /><applet load="1i6a" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1i6a, resolution 2.3Å" />

'''CRYSTAL STUCTURE OF THE OXIDIZED FORM OF OXYR'''<br />

==Overview==

The Escherichia coli OxyR transcription factor senses H2O2 and is, activated through the formation of an intramolecular disulfide bond. Here, we present the crystal structures of the regulatory domain of OxyR in its, reduced and oxidized forms, determined at 2.7 A and 2.3 A resolutions, respectively. In the reduced form, the two redox-active cysteines are, separated by approximately 17 A. Disulfide bond formation in the oxidized, form results in a significant structural change in the regulatory domain., The structural remodeling, which leads to different oligomeric, associations, accounts for the redox-dependent switch in OxyR and provides, a novel example of protein regulation by "fold editing" through a, reversible disulfide bond formation within a folded domain.

The Escherichia coli OxyR transcription factor senses H2O2 and is activated through the formation of an intramolecular disulfide bond. Here we present the crystal structures of the regulatory domain of OxyR in its reduced and oxidized forms, determined at 2.7 A and 2.3 A resolutions, respectively. In the reduced form, the two redox-active cysteines are separated by approximately 17 A. Disulfide bond formation in the oxidized form results in a significant structural change in the regulatory domain. The structural remodeling, which leads to different oligomeric associations, accounts for the redox-dependent switch in OxyR and provides a novel example of protein regulation by "fold editing" through a reversible disulfide bond formation within a folded domain.

==About this Structure==

1I6A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1I6A OCA].

1I6A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I6A OCA].

==Reference==

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[[Category: oxyr regulatory domain]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 17~~:05:~~09 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:08:22 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1i6a.jpg|left|200px]]<br /><applet load="1i6a" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1i6a.jpg|left|200px]]<br /><applet load="1i6a" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1i6a, resolution 2.3&Aring;" />
 '''CRYSTAL STUCTURE OF THE OXIDIZED FORM OF OXYR'''<br />
 ==Overview==
-The Escherichia coli OxyR transcription factor senses H2O2 and is, activated through the formation of an intramolecular disulfide bond. Here, we present the crystal structures of the regulatory domain of OxyR in its, reduced and oxidized forms, determined at 2.7 A and 2.3 A resolutions, respectively. In the reduced form, the two redox-active cysteines are, separated by approximately 17 A. Disulfide bond formation in the oxidized, form results in a significant structural change in the regulatory domain., The structural remodeling, which leads to different oligomeric, associations, accounts for the redox-dependent switch in OxyR and provides, a novel example of protein regulation by "fold editing" through a, reversible disulfide bond formation within a folded domain.
+The Escherichia coli OxyR transcription factor senses H2O2 and is activated through the formation of an intramolecular disulfide bond. Here we present the crystal structures of the regulatory domain of OxyR in its reduced and oxidized forms, determined at 2.7 A and 2.3 A resolutions, respectively. In the reduced form, the two redox-active cysteines are separated by approximately 17 A. Disulfide bond formation in the oxidized form results in a significant structural change in the regulatory domain. The structural remodeling, which leads to different oligomeric associations, accounts for the redox-dependent switch in OxyR and provides a novel example of protein regulation by "fold editing" through a reversible disulfide bond formation within a folded domain.
 ==About this Structure==
-I6A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1I6A OCA].
+I6A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I6A OCA].
 ==Reference==
@@ Line 19: / Line 19: @@
 [[Category: oxyr regulatory domain]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:05:09 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:08:22 2008''