2c3p: Difference between revisions

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[[Image:2c3p.gif|left|200px]]
{{Seed}}
[[Image:2c3p.png|left|200px]]


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{{STRUCTURE_2c3p|  PDB=2c3p  |  SCENE=  }}  
{{STRUCTURE_2c3p|  PDB=2c3p  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF THE FREE RADICAL INTERMEDIATE OF PYRUVATE:FERREDOXIN OXIDOREDUCTASE FROM DESULFOVIBRIO AFRICANUS'''
===CRYSTAL STRUCTURE OF THE FREE RADICAL INTERMEDIATE OF PYRUVATE:FERREDOXIN OXIDOREDUCTASE FROM DESULFOVIBRIO AFRICANUS===




==Overview==
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Pyruvate-ferredoxin oxidoreductases (PFOR) are unique among thiamine pyrophosphate (ThDP)-containing enzymes in giving rise to a rather stable cofactor-based free-radical species upon the decarboxylation of their first substrate, pyruvate. We have obtained snapshots of unreacted and partially reacted (probably as a tetrahedral intermediate) pyruvate-PFOR complexes at different time intervals. We conclude that pyruvate decarboxylation involves very limited substrate-to-product movements but a significant displacement of the thiazolium moiety of ThDP. In this respect, PFOR seems to differ substantially from other ThDP-containing enzymes, such as transketolase and pyruvate decarboxylase. In addition, exposure of PFOR to oxygen in the presence of pyruvate results in significant inhibition of catalytic activity, both in solution and in the crystals. Examination of the crystal structure of inhibited PFOR suggests that the loss of activity results from oxime formation at the 4' amino substituent of the pyrimidine moiety of ThDP.
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{{ABSTRACT_PUBMED_16472741}}


==About this Structure==
==About this Structure==
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[[Category: Pyruvate catabolism]]
[[Category: Pyruvate catabolism]]
[[Category: Tpp-dependent enzyme]]
[[Category: Tpp-dependent enzyme]]
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Revision as of 23:47, 28 July 2008

File:2c3p.png

Template:STRUCTURE 2c3p

CRYSTAL STRUCTURE OF THE FREE RADICAL INTERMEDIATE OF PYRUVATE:FERREDOXIN OXIDOREDUCTASE FROM DESULFOVIBRIO AFRICANUS

Template:ABSTRACT PUBMED 16472741

About this Structure

2C3P is a Single protein structure of sequence from Desulfovibrio africanus. Full crystallographic information is available from OCA.

Reference

Flexibility of thiamine diphosphate revealed by kinetic crystallographic studies of the reaction of pyruvate-ferredoxin oxidoreductase with pyruvate., Cavazza C, Contreras-Martel C, Pieulle L, Chabriere E, Hatchikian EC, Fontecilla-Camps JC, Structure. 2006 Feb;14(2):217-24. PMID:16472741

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