View source for 1kek


==Crystal Structure of the Free Radical Intermediate of Pyruvate:Ferredoxin Oxidoreductase==
<StructureSection load='1kek' size='340' side='right'caption='[[1kek]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1kek]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Desulfovibrio_africanus Desulfovibrio 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>
</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=CO2:CARBON+DIOXIDE'>CO2</scene>, <scene name='pdbligand=HTL:2-ACETYL-THIAMINE+DIPHOSPHATE'>HTL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1b0p|1b0p]], [[2pda|2pda]]</div></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Pyruvate_synthase Pyruvate synthase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.7.1 1.2.7.1] </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=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>
</table>
== Function ==
[[https://www.uniprot.org/uniprot/P94692_DESAF P94692_DESAF]] Oxidoreductase required for the transfer of electrons from pyruvate to flavodoxin (By similarity).[PIRNR:PIRNR000159] 
== 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/ke/1kek_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=1kek ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1kek" style="background-color:#fffaf0;"></div>

==See Also==
*[[Pyruvate-ferredoxin oxidoreductase|Pyruvate-ferredoxin oxidoreductase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Desulfovibrio africanus]]
[[Category: Large Structures]]
[[Category: Pyruvate synthase]]
[[Category: Chabriere, E]]
[[Category: Charon, M H]]
[[Category: Fontecilla-Camps, J C]]
[[Category: Guigliarelli, B]]
[[Category: Hatchikian, E C]]
[[Category: Vernede, X]]
[[Category: Domain]]
[[Category: Homodimer]]
[[Category: Oxidoreductase]]