1kek

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[[Image:1kek.gif|left|200px]]<br /><applet load="1kek" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1kek.gif|left|200px]]
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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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{{Structure
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|PDB= 1kek |SIZE=350|CAPTION= <scene name='initialview01'>1kek</scene>, resolution 1.90&Aring;
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|SITE=
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|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>
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|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]
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|GENE=
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}}
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'''Crystal Structure of the Free Radical Intermediate of Pyruvate:Ferredoxin Oxidoreductase'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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 <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=SF4:'>SF4</scene>, <scene name='pdbligand=HTL:'>HTL</scene> and <scene name='pdbligand=CO2:'>CO2</scene> 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1KEK OCA].
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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==
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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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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]]
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[[Category: 7 domains]]
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[[Category: 7 domain]]
[[Category: homodimer]]
[[Category: homodimer]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:33:16 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:16:20 2008''

Revision as of 10:16, 20 March 2008

Image:1kek.gif


PDB ID 1kek

Drag the structure with the mouse to rotate
, resolution 1.90Å
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


Overview

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 Structure

1KEK is a Single protein structure of sequence from Desulfovibrio africanus. Full crystallographic information is available from OCA.

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:11752578

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