1vzh: Difference between revisions

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-[[Image:1vzh.gif|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_1vzh", creates the "Structure Box" on the page.
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-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-or leave the SCENE parameter empty for the default display.
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-{{STRUCTURE_1vzh|  PDB=1vzh  |  SCENE=  }}
-'''STRUCTURE OF SUPEROXIDE REDUCTASE BOUND TO FERROCYANIDE AND ACTIVE SITE EXPANSION UPON X-RAY INDUCED PHOTOREDUCTION'''
+==Structure of superoxide reductase bound to ferrocyanide and active site expansion upon X-ray induced photoreduction==
+<StructureSection load='1vzh' size='340' side='right'caption='[[1vzh]], [[Resolution|resolution]] 1.69&Aring;' scene=''>
+== Structural highlights ==
+<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.69&#8491;</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=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>
+</table>
+== 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 ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vz/1vzh_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=1vzh ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== 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.
-==Overview==
+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>
-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.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-VZH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_baarsii Desulfovibrio baarsii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VZH OCA].
+</div>
+<div class="pdbe-citations 1vzh" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-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://www.ncbi.nlm.nih.gov/pubmed/15341736 15341736]
+*[[Superoxide Reductase|Superoxide Reductase]]
-[[Category: Desulfovibrio baarsii]]
+== References ==
-[[Category: Single protein]]
+<references/>
-[[Category: Superoxide reductase]]
+__TOC__
-[[Category: Adam, V.]]
+</StructureSection>
-[[Category: Bourgeois, D.]]
+[[Category: Desulfarculus baarsii]]
-[[Category: Molina-Heredia, F P.]]
+[[Category: Large Structures]]
-[[Category: Niviere, V.]]
+[[Category: Adam V]]
-[[Category: Royant, A.]]
+[[Category: Bourgeois D]]
-[[Category: Dinuclear iron cluster]]
+[[Category: Molina-Heredia FP]]
-[[Category: Electron transport]]
+[[Category: Niviere V]]
-[[Category: Ferrocyanide]]
+[[Category: Royant A]]
-[[Category: Microspectrophotometry]]
-[[Category: Oxidoreductase]]
-[[Category: Photoreduction]]
-[[Category: Redox state]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 12:57:13 2008''