1i6a: Difference between revisions
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<StructureSection load='1i6a' size='340' side='right' caption='[[1i6a]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='1i6a' size='340' side='right' caption='[[1i6a]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1i6a]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1i6a]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I6A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1I6A FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1i69|1i69]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1i69|1i69]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1i6a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i6a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1i6a RCSB], [http://www.ebi.ac.uk/pdbsum/1i6a PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1i6a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i6a OCA], [http://pdbe.org/1i6a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1i6a RCSB], [http://www.ebi.ac.uk/pdbsum/1i6a PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1i6a" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Bacillus coli migula 1895]] | ||
[[Category: Choi, H]] | [[Category: Choi, H]] | ||
[[Category: Kim, S]] | [[Category: Kim, S]] | ||
Revision as of 09:56, 11 September 2015
CRYSTAL STUCTURE OF THE OXIDIZED FORM OF OXYRCRYSTAL STUCTURE OF THE OXIDIZED FORM OF OXYR
Structural highlights
Function[OXYR_ECOLI] Hydrogen peroxide sensor. Activates the expression of a regulon of hydrogen peroxide-inducible genes such as katG, gor, ahpC, ahpF, oxyS (a regulatory RNA), dps, fur and grxA. OxyR expression is negatively autoregulated by binding to a 43 bp region upstream of its own coding sequence. OxyR is inactivated by reduction of its essential disulfide bond by the product of GrxA, itself positively regulated by OxyR. Has also a positive regulatory effect on the production of surface proteins that control the colony morphology and auto-aggregation ability. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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