1i6a: Difference between revisions

Revision as of 19:37, 2 May 2008

CRYSTAL STUCTURE OF THE OXIDIZED FORM OF OXYR

OverviewOverview

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 StructureAbout this Structure

1I6A is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

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 Page seeded by OCA on Fri May 2 19:37:18 2008

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OCA

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 '''CRYSTAL STUCTURE OF THE OXIDIZED FORM OF OXYR'''
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 [[Category: Kim, S.]]
 [[Category: Ryu, S.]]
-[[Category: oxidized form]]
+[[Category: Oxidized form]]
-[[Category: oxyr regulatory domain]]
+[[Category: Oxyr regulatory domain]]
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 19:37:18 2008''
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:15:10 2008''