2c3p

File:2c3p.gif

spinqualitylabelsall models 2c3p, resolution 2.33Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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

OverviewOverview

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 StructureAbout this Structure

2C3P is a [Single protein] structure of sequence from [Desulfovibrio africanus] with MG, CA, SF4 and 1TP as [ligands]. Active as [Pyruvate synthase], with EC number [1.2.7.1]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

ReferenceReference

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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