2c3y
CRYSTAL STRUCTURE OF THE RADICAL FORM OF PYRUVATE:FERREDOXIN OXIDOREDUCTASE FROM DESULFOVIBRIO AFRICANUS
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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
2C3Y is a [Single protein] structure of sequence from [Desulfovibrio africanus] with MG, CA, SF4, HTL and CO2 as [ligands]. Active as [[1]], with EC number [1.2.7.1]. 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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