1b0p

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(New page: 200px<br /><applet load="1b0p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b0p, resolution 2.31&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1b0p.gif|left|200px]]<br /><applet load="1b0p" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1b0p, resolution 2.31&Aring;" />
 
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'''CRYSTAL STRUCTURE OF PYRUVATE-FERREDOXIN OXIDOREDUCTASE FROM DESULFOVIBRIO AFRICANUS'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF PYRUVATE-FERREDOXIN OXIDOREDUCTASE FROM DESULFOVIBRIO AFRICANUS==
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Oxidative decarboxylation of pyruvate to form acetyl-coenzyme A, a crucial, step in many metabolic pathways, is carried out in most aerobic organisms, by the multienzyme complex pyruvate dehydrogenase. In most anaerobes, the, same reaction is usually catalyzed by a single enzyme, pyruvate:ferredoxin, oxidoreductase (PFOR). Thus, PFOR is a potential target for drug design, against certain anaerobic pathogens. Here, we report the crystal, structures of the homodimeric Desulfovibrio africanus PFOR (data to 2.3 A, resolution), and of its complex with pyruvate (3.0 A resolution). The, structures show that each subunit consists of seven domains, one of which, affords protection against oxygen. The thiamin pyrophosphate (TPP), cofactor and the three [4Fe-4S] clusters are suitably arranged to provide, a plausible electron transfer pathway. In addition, the PFOR-pyruvate, complex structure shows the noncovalent fixation of the substrate before, the catalytic reaction.
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<StructureSection load='1b0p' size='340' side='right'caption='[[1b0p]], [[Resolution|resolution]] 2.31&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1b0p]] 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=1B0P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B0P 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]] 2.31&#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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</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=1b0p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b0p OCA], [https://pdbe.org/1b0p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b0p RCSB], [https://www.ebi.ac.uk/pdbsum/1b0p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b0p 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/b0/1b0p_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=1b0p 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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Oxidative decarboxylation of pyruvate to form acetyl-coenzyme A, a crucial step in many metabolic pathways, is carried out in most aerobic organisms by the multienzyme complex pyruvate dehydrogenase. In most anaerobes, the same reaction is usually catalyzed by a single enzyme, pyruvate:ferredoxin oxidoreductase (PFOR). Thus, PFOR is a potential target for drug design against certain anaerobic pathogens. Here, we report the crystal structures of the homodimeric Desulfovibrio africanus PFOR (data to 2.3 A resolution), and of its complex with pyruvate (3.0 A resolution). The structures show that each subunit consists of seven domains, one of which affords protection against oxygen. The thiamin pyrophosphate (TPP) cofactor and the three [4Fe-4S] clusters are suitably arranged to provide a plausible electron transfer pathway. In addition, the PFOR-pyruvate complex structure shows the noncovalent fixation of the substrate before the catalytic reaction.
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==About this Structure==
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Crystal structures of the key anaerobic enzyme pyruvate:ferredoxin oxidoreductase, free and in complex with pyruvate.,Chabriere E, Charon MH, Volbeda A, Pieulle L, Hatchikian EC, Fontecilla-Camps JC Nat Struct Biol. 1999 Feb;6(2):182-90. PMID:10048931<ref>PMID:10048931</ref>
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1B0P 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 and TPP 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=1B0P 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 structures of the key anaerobic enzyme pyruvate:ferredoxin oxidoreductase, free and in complex with pyruvate., Chabriere E, Charon MH, Volbeda A, Pieulle L, Hatchikian EC, Fontecilla-Camps JC, Nat Struct Biol. 1999 Feb;6(2):182-90. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10048931 10048931]
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</div>
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[[Category: Desulfovibrio africanus]]
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<div class="pdbe-citations 1b0p" 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: Volbeda, A.]]
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[[Category: CA]]
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[[Category: MG]]
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[[Category: SF4]]
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[[Category: TPP]]
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[[Category: iron-sulfur cluster]]
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[[Category: oxidoreductase]]
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[[Category: pyruvate catabolism]]
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[[Category: tpp-dependent enzyme]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 23:34:30 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 MH]]
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[[Category: Volbeda A]]

Current revision

CRYSTAL STRUCTURE OF PYRUVATE-FERREDOXIN OXIDOREDUCTASE FROM DESULFOVIBRIO AFRICANUS

PDB ID 1b0p

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