1vzh: Difference between revisions
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<StructureSection load='1vzh' size='340' side='right'caption='[[1vzh]], [[Resolution|resolution]] 1.69Å' scene=''> | <StructureSection load='1vzh' size='340' side='right'caption='[[1vzh]], [[Resolution|resolution]] 1.69Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1vzh]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VZH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VZH FirstGlance]. <br> | <table><tr><td colspan='2'>[[1vzh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Desulfarculus_baarsii Desulfarculus baarsii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VZH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VZH FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.69Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FC6:HEXACYANOFERRATE(3-)'>FC6</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></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=1vzh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vzh OCA], [https://pdbe.org/1vzh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vzh RCSB], [https://www.ebi.ac.uk/pdbsum/1vzh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vzh 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=1vzh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vzh OCA], [https://pdbe.org/1vzh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vzh RCSB], [https://www.ebi.ac.uk/pdbsum/1vzh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vzh ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/DFX_DESB2 DFX_DESB2] Catalyzes the one-electron reduction of superoxide anion radical to hydrogen peroxide at a nonheme ferrous iron center. Plays a fundamental role in case of oxidative stress via its superoxide detoxification activity.<ref>PMID:10617593</ref> | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Desulfarculus baarsii]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Adam V]] | |||
[[Category: Adam | [[Category: Bourgeois D]] | ||
[[Category: Bourgeois | [[Category: Molina-Heredia FP]] | ||
[[Category: Molina-Heredia | [[Category: Niviere V]] | ||
[[Category: Niviere | [[Category: Royant A]] | ||
[[Category: Royant | |||
Latest revision as of 16:09, 13 December 2023
Structure of superoxide reductase bound to ferrocyanide and active site expansion upon X-ray induced photoreductionStructure of superoxide reductase bound to ferrocyanide and active site expansion upon X-ray induced photoreduction
Structural highlights
FunctionDFX_DESB2 Catalyzes the one-electron reduction of superoxide anion radical to hydrogen peroxide at a nonheme ferrous iron center. Plays a fundamental role in case of oxidative stress via its superoxide detoxification activity.[1] 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 PubMedSome sulfate-reducing and microaerophilic bacteria rely on the enzyme superoxide reductase (SOR) to eliminate the toxic superoxide anion radical (O2*-). SOR catalyses the one-electron reduction of O2*- to hydrogen peroxide at a nonheme ferrous iron center. The structures of Desulfoarculus baarsii SOR (mutant E47A) alone and in complex with ferrocyanide were solved to 1.15 and 1.7 A resolution, respectively. The latter structure, the first ever reported of a complex between ferrocyanide and a protein, reveals that this organo-metallic compound entirely plugs the SOR active site, coordinating the active iron through a bent cyano bridge. The subtle structural differences between the mixed-valence and the fully reduced SOR-ferrocyanide adducts were investigated by taking advantage of the photoelectrons induced by X-rays. The results reveal that photo-reduction from Fe(III) to Fe(II) of the iron center, a very rapid process under a powerful synchrotron beam, induces an expansion of the SOR active site. Structure of superoxide reductase bound to ferrocyanide and active site expansion upon X-ray-induced photo-reduction.,Adam V, Royant A, Niviere V, Molina-Heredia FP, Bourgeois D Structure. 2004 Sep;12(9):1729-40. PMID:15341736[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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