1kek: Difference between revisions
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[[Image:1kek.gif|left|200px]] | [[Image:1kek.gif|left|200px]] | ||
'''Crystal Structure of the Free Radical Intermediate of Pyruvate:Ferredoxin Oxidoreductase''' | {{Structure | ||
|PDB= 1kek |SIZE=350|CAPTION= <scene name='initialview01'>1kek</scene>, resolution 1.90Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=HTL:2-ACETYL-THIAMINE+DIPHOSPHATE'>HTL</scene> and <scene name='pdbligand=CO2:CARBON DIOXIDE'>CO2</scene> | |||
|ACTIVITY= [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] | |||
|GENE= | |||
}} | |||
'''Crystal Structure of the Free Radical Intermediate of Pyruvate:Ferredoxin Oxidoreductase''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1KEK is a [ | 1KEK is a [[Single protein]] structure of sequence from [http://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]. | ||
==Reference== | ==Reference== | ||
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:// | 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://www.ncbi.nlm.nih.gov/pubmed/11752578 11752578] | ||
[[Category: Desulfovibrio africanus]] | [[Category: Desulfovibrio africanus]] | ||
[[Category: Pyruvate synthase]] | [[Category: Pyruvate synthase]] | ||
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[[Category: MG]] | [[Category: MG]] | ||
[[Category: SF4]] | [[Category: SF4]] | ||
[[Category: 7 | [[Category: 7 domain]] | ||
[[Category: homodimer]] | [[Category: homodimer]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:16:20 2008'' |
Revision as of 13:16, 20 March 2008
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, resolution 1.90Å | |||||||
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Ligands: | , , , and | ||||||
Activity: | Pyruvate synthase, with EC number 1.2.7.1 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Crystal Structure of the Free Radical Intermediate of Pyruvate:Ferredoxin Oxidoreductase
OverviewOverview
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.
About this StructureAbout this Structure
1KEK is a Single protein structure of sequence from Desulfovibrio africanus. Full crystallographic information is available from OCA.
ReferenceReference
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
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