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2c3u
From Proteopedia
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CRYSTAL STRUCTURE OF PYRUVATE-FERREDOXIN OXIDOREDUCTASE FROM DESULFOVIBRIO AFRICANUS, OXYGEN INHIBITED FORM
Overview
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 ... [(full description)]
About this Structure
2C3U is a [Single protein] structure of sequence from [Desulfovibrio africanus] with MG, CA, SF4, 2TP and PYR as [ligands]. Active as [[1]], with EC number [1.2.7.1]. 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
Page seeded by OCA on Mon Oct 29 18:56:27 2007
Categories: Desulfovibrio africanus | Single protein | Cavazza, C. | Chabriere, E. | Contreras-Martel, C. | Fontecilla-Camps, J.C. | Hatchikian, E.C. | Pieulle, L. | 2TP | CA | MG | PYR | SF4 | 4fe-4s | Electron transport | Iron | Iron-sulfur | Iron-sulfur cluster | Metal-binding | Oxidoreductase | Pyruvate catabolism | Tpp-dependent enzyme
