1kek

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(New page: 200px<br /><applet load="1kek" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kek, resolution 1.90&Aring;" /> '''Crystal Structure of...)
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[[Image:1kek.gif|left|200px]]<br /><applet load="1kek" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1kek, resolution 1.90&Aring;" />
 
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'''Crystal Structure of the Free Radical Intermediate of Pyruvate:Ferredoxin Oxidoreductase'''<br />
 
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==Overview==
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==Crystal Structure of the Free Radical Intermediate of Pyruvate:Ferredoxin Oxidoreductase==
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In anaerobic organisms, the decarboxylation of pyruvate, a crucial, component of intermediary metabolism, is catalyzed by the metalloenzyme, pyruvate: ferredoxin oxidoreductase (PFOR) resulting in the generation of, low potential electrons and the subsequent acetylation of coenzyme A, (CoA). PFOR is the only enzyme for which a stable acetyl thiamine, diphosphate (ThDP)-based free radical reaction intermediate has been, identified. The 1.87 A-resolution structure of the radical form of PFOR, from Desulfovibrio africanus shows that, despite currently accepted ideas, the thiazole ring of the ThDP cofactor is markedly bent, indicating a, drastic reduction of its aromaticity. In addition, the bond connecting the, acetyl group to ThDP is unusually long, probably of the one-electron type, already described for several cation radicals but not yet found in a, biological system. Taken together, our data, along with evidence from the, literature, suggest that acetyl-CoA synthesis by PFOR proceeds via a, condensation mechanism involving acetyl (PFOR-based) and thiyl (CoA-based), radicals.
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<StructureSection load='1kek' size='340' side='right'caption='[[1kek]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1kek]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Desulfocurvibacter_africanus Desulfocurvibacter africanus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KEK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KEK 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]] 1.9&#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=CO2:CARBON+DIOXIDE'>CO2</scene>, <scene name='pdbligand=HTL:2-ACETYL-THIAMINE+DIPHOSPHATE'>HTL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=1kek FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kek OCA], [https://pdbe.org/1kek PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kek RCSB], [https://www.ebi.ac.uk/pdbsum/1kek PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kek ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PFOR_DESAF PFOR_DESAF] Catalyzes the ferredoxin-dependent oxidative decarboxylation of pyruvate. Required for the transfer of electrons from pyruvate to ferredoxin (PubMed:9294422, PubMed:7612653). Ferredoxin I and ferredoxin II, which are single 4Fe-4S cluster ferredoxins are the most effective electron carriers of POR (PubMed:7612653).<ref>PMID:7612653</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/ke/1kek_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1kek 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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In anaerobic organisms, the decarboxylation of pyruvate, a crucial component of intermediary metabolism, is catalyzed by the metalloenzyme pyruvate: ferredoxin oxidoreductase (PFOR) resulting in the generation of low potential electrons and the subsequent acetylation of coenzyme A (CoA). PFOR is the only enzyme for which a stable acetyl thiamine diphosphate (ThDP)-based free radical reaction intermediate has been identified. The 1.87 A-resolution structure of the radical form of PFOR from Desulfovibrio africanus shows that, despite currently accepted ideas, the thiazole ring of the ThDP cofactor is markedly bent, indicating a drastic reduction of its aromaticity. In addition, the bond connecting the acetyl group to ThDP is unusually long, probably of the one-electron type already described for several cation radicals but not yet found in a biological system. Taken together, our data, along with evidence from the literature, suggest that acetyl-CoA synthesis by PFOR proceeds via a condensation mechanism involving acetyl (PFOR-based) and thiyl (CoA-based) radicals.
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==About this Structure==
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Crystal structure of the free radical intermediate of pyruvate:ferredoxin oxidoreductase.,Chabriere E, Vernede X, Guigliarelli B, Charon MH, Hatchikian EC, Fontecilla-Camps JC Science. 2001 Dec 21;294(5551):2559-63. PMID:11752578<ref>PMID:11752578</ref>
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1KEK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_africanus Desulfovibrio africanus] with MG, CA, SF4, HTL and CO2 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Pyruvate_synthase Pyruvate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.7.1 1.2.7.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KEK 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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Crystal structure of the free radical intermediate of pyruvate:ferredoxin oxidoreductase., Chabriere E, Vernede X, Guigliarelli B, Charon MH, Hatchikian EC, Fontecilla-Camps JC, Science. 2001 Dec 21;294(5551):2559-63. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11752578 11752578]
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</div>
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[[Category: Desulfovibrio africanus]]
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<div class="pdbe-citations 1kek" style="background-color:#fffaf0;"></div>
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[[Category: Pyruvate synthase]]
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[[Category: Single protein]]
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[[Category: Chabriere, E.]]
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[[Category: Charon, M.H.]]
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[[Category: Fontecilla-Camps, J.C.]]
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[[Category: Guigliarelli, B.]]
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[[Category: Hatchikian, E.C.]]
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[[Category: Vernede, X.]]
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[[Category: CA]]
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[[Category: CO2]]
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[[Category: HTL]]
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[[Category: MG]]
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[[Category: SF4]]
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[[Category: 7 domains]]
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[[Category: homodimer]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 01:13:23 2007''
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==See Also==
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*[[Pyruvate-ferredoxin oxidoreductase|Pyruvate-ferredoxin oxidoreductase]]
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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: Desulfocurvibacter africanus]]
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[[Category: Large Structures]]
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[[Category: Chabriere E]]
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[[Category: Charon M-H]]
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[[Category: Fontecilla-Camps JC]]
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[[Category: Guigliarelli B]]
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[[Category: Hatchikian EC]]
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[[Category: Vernede X]]

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Crystal Structure of the Free Radical Intermediate of Pyruvate:Ferredoxin Oxidoreductase

PDB ID 1kek

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