1vzi

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[[Image:1vzi.gif|left|200px]]<br />
 
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<applet load="1vzi" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1vzi, resolution 1.15&Aring;" />
 
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'''STRUCTURE OF SUPEROXIDE REDUCTASE BOUND TO FERROCYANIDE AND ACTIVE SITE EXPANSION UPON X-RAY INDUCED PHOTOREDUCTION'''<br />
 
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==Overview==
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==Structure of superoxide reductase bound to ferrocyanide and active site expansion upon X-ray induced photoreduction==
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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.
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<StructureSection load='1vzi' size='340' side='right'caption='[[1vzi]], [[Resolution|resolution]] 1.15&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.15&#8491;</td></tr>
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<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>
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<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>
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vz/1vzi_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1vzi ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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<ref>PMID:15341736</ref>
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1VZI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_baarsii Desulfovibrio baarsii] with CA, CL and FE2 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Superoxide_reductase Superoxide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.2 1.15.1.2] Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1VZI OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15341736 15341736]
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</div>
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[[Category: Desulfovibrio baarsii]]
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<div class="pdbe-citations 1vzi" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Superoxide reductase]]
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[[Category: Adam, V.]]
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[[Category: Bourgeois, D.]]
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[[Category: Molina-Heredia, F.P.]]
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[[Category: Niviere, V.]]
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[[Category: Royant, A.]]
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[[Category: CA]]
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[[Category: CL]]
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[[Category: FE2]]
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[[Category: dinuclear iron cluster]]
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[[Category: electron transport]]
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[[Category: ferrocyanide]]
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[[Category: microspectrophotometry]]
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[[Category: oxidoreductase]]
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[[Category: photoreduction]]
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[[Category: redox states]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 15:20:03 2007''
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==See Also==
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*[[Superoxide Reductase|Superoxide Reductase]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Desulfarculus baarsii]]
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[[Category: Large Structures]]
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[[Category: Adam V]]
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[[Category: Bourgeois D]]
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[[Category: Molina-Heredia FP]]
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[[Category: Niviere V]]
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[[Category: Royant A]]

Current revision

Structure of superoxide reductase bound to ferrocyanide and active site expansion upon X-ray induced photoreduction

PDB ID 1vzi

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