1i6a
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(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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Revision as of 14:57, 20 November 2007
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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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