1i69

From Proteopedia

(Difference between revisions)

Revision as of 10:57, 4 August 2021

CRYSTAL STRUCTURE OF THE REDUCED FORM OF OXYR

Structural highlights

1i69 is a 2 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1i6a
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 PubMed

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.

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

↑ Choi H, Kim S, Mukhopadhyay P, Cho S, Woo J, Storz G, Ryu S. Structural basis of the redox switch in the OxyR transcription factor. Cell. 2001 Apr 6;105(1):103-13. PMID:11301006

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1i69"

@@ Line 3: / Line 3: @@
 <StructureSection load='1i69' size='340' side='right'caption='[[1i69]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1i69]] is a 2 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=1I69 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1I69 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1i69]] is a 2 chain structure with sequence from [https://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=1I69 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I69 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BEZ:BENZOIC+ACID'>BEZ</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BEZ:BENZOIC+ACID'>BEZ</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1i6a|1i6a]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1i6a|1i6a]]</div></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=1i69 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i69 OCA], [http://pdbe.org/1i69 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1i69 RCSB], [http://www.ebi.ac.uk/pdbsum/1i69 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1i69 ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1i69 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i69 OCA], [https://pdbe.org/1i69 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i69 RCSB], [https://www.ebi.ac.uk/pdbsum/1i69 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i69 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/OXYR_ECOLI 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.
+[[https://www.uniprot.org/uniprot/OXYR_ECOLI 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 ==
 [[Image:Consurf_key_small.gif|200px|right]]

1i69

From Proteopedia

Revision as of 10:57, 4 August 2021

CRYSTAL STRUCTURE OF THE REDUCED FORM OF OXYR

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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