1kek

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[[Image:1kek.gif|left|200px]]
[[Image:1kek.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1kek |SIZE=350|CAPTION= <scene name='initialview01'>1kek</scene>, resolution 1.90&Aring;
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The line below this paragraph, containing "STRUCTURE_1kek", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <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>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_1kek| PDB=1kek | SCENE= }}
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|RELATEDENTRY=[[1b0p|1B0P]], [[2pda|2PDA]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kek FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kek OCA], [http://www.ebi.ac.uk/pdbsum/1kek PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1kek RCSB]</span>
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}}
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'''Crystal Structure of the Free Radical Intermediate of Pyruvate:Ferredoxin Oxidoreductase'''
'''Crystal Structure of the Free Radical Intermediate of Pyruvate:Ferredoxin Oxidoreductase'''
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[[Category: Vernede, X.]]
[[Category: Vernede, X.]]
[[Category: 7 domain]]
[[Category: 7 domain]]
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[[Category: homodimer]]
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[[Category: Homodimer]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:38:49 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:47:27 2008''
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Revision as of 19:38, 2 May 2008

Image:1kek.gif

Template:STRUCTURE 1kek

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 Page seeded by OCA on Fri May 2 22:38:49 2008

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