1i6a
From Proteopedia
(New page: 200px<br /><applet load="1i6a" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i6a, resolution 2.3Å" /> '''CRYSTAL STUCTURE OF T...) |
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| - | [[Image:1i6a.jpg|left|200px]]<br /><applet load="1i6a" size=" | + | [[Image:1i6a.jpg|left|200px]]<br /><applet load="1i6a" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1i6a, resolution 2.3Å" /> | caption="1i6a, resolution 2.3Å" /> | ||
'''CRYSTAL STUCTURE OF THE OXIDIZED FORM OF OXYR'''<br /> | '''CRYSTAL STUCTURE OF THE OXIDIZED FORM OF OXYR'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The Escherichia coli OxyR transcription factor senses H2O2 and is | + | 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== | ==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:// | + | 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== | ==Reference== | ||
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[[Category: oxyr regulatory domain]] | [[Category: oxyr regulatory domain]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:08:22 2008'' |
Revision as of 11:08, 21 February 2008
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CRYSTAL STUCTURE OF THE OXIDIZED FORM OF OXYR
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.
About this Structure
1I6A is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structural basis of the redox switch in the OxyR transcription factor., Choi H, Kim S, Mukhopadhyay P, Cho S, Woo J, Storz G, Ryu S, Cell. 2001 Apr 6;105(1):103-13. PMID:11301006
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