This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1kek
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1kek.gif|left|200px]] | [[Image:1kek.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1kek", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | | | + | --> |
| - | | | + | {{STRUCTURE_1kek| PDB=1kek | SCENE= }} |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''Crystal Structure of the Free Radical Intermediate of Pyruvate:Ferredoxin Oxidoreductase''' | '''Crystal Structure of the Free Radical Intermediate of Pyruvate:Ferredoxin Oxidoreductase''' | ||
| Line 33: | Line 30: | ||
[[Category: Vernede, X.]] | [[Category: Vernede, X.]] | ||
[[Category: 7 domain]] | [[Category: 7 domain]] | ||
| - | [[Category: | + | [[Category: Homodimer]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:38:49 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 19:38, 2 May 2008
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
