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| | <StructureSection load='1vzi' size='340' side='right'caption='[[1vzi]], [[Resolution|resolution]] 1.15Å' scene=''> | | <StructureSection load='1vzi' size='340' side='right'caption='[[1vzi]], [[Resolution|resolution]] 1.15Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1vzi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_33931 Atcc 33931]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VZI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VZI FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1vzi]] 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=1VZI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VZI FirstGlance]. <br> |
| - | </td></tr><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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.15Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1vzh|1vzh]], [[1vzg|1vzg]]</div></td></tr> | + | <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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Superoxide_reductase Superoxide reductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.2 1.15.1.2] </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=1vzi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vzi OCA], [https://pdbe.org/1vzi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vzi RCSB], [https://www.ebi.ac.uk/pdbsum/1vzi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vzi 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=1vzi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vzi OCA], [https://pdbe.org/1vzi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vzi RCSB], [https://www.ebi.ac.uk/pdbsum/1vzi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vzi 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>
| + | [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: Atcc 33931]] | + | [[Category: Desulfarculus baarsii]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Superoxide reductase]]
| + | [[Category: Adam V]] |
| - | [[Category: Adam, V]] | + | [[Category: Bourgeois D]] |
| - | [[Category: Bourgeois, D]] | + | [[Category: Molina-Heredia FP]] |
| - | [[Category: Molina-Heredia, F P]] | + | [[Category: Niviere V]] |
| - | [[Category: Niviere, V]] | + | [[Category: Royant A]] |
| - | [[Category: Royant, A]] | + | |
| - | [[Category: Dinuclear iron cluster]]
| + | |
| - | [[Category: Electron transport]]
| + | |
| - | [[Category: Ferrocyanide]]
| + | |
| - | [[Category: Microspectrophotometry]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Photoreduction]]
| + | |
| - | [[Category: Redox state]]
| + | |
| Structural highlights
Function
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.[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 PubMed
Some 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 Also
References
- ↑ Lombard M, Fontecave M, Touati D, Niviere V. Reaction of the desulfoferrodoxin from Desulfoarculus baarsii with superoxide anion. Evidence for a superoxide reductase activity. J Biol Chem. 2000 Jan 7;275(1):115-21. PMID:10617593
- ↑ Adam V, Royant A, Niviere V, Molina-Heredia FP, Bourgeois D. Structure of superoxide reductase bound to ferrocyanide and active site expansion upon X-ray-induced photo-reduction. Structure. 2004 Sep;12(9):1729-40. PMID:15341736 doi:10.1016/j.str.2004.07.013
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