Crystallization and preliminary crystallographic analysis of the pyruvate-ferredoxin oxidoreductase from Desulfovibrio africanus

L Pieulle; E Chabrière; C Hatchikian; J C Fontecilla-Camps; M H Charon

doi:10.1107/S0907444998008920

Crystallization and preliminary crystallographic analysis of the pyruvate-ferredoxin oxidoreductase from Desulfovibrio africanus

Acta Crystallogr D Biol Crystallogr. 1999 Jan;55(Pt 1):329-31. doi: 10.1107/S0907444998008920. Epub 1999 Jan 1.

Authors

L Pieulle¹, E Chabrière, C Hatchikian, J C Fontecilla-Camps, M H Charon

Affiliation

¹ Unité de Bioénergétique et Ingénierie des Protéines, CNRS, 31 Chemin Joseph Aiguier, F-13402 Marseille CEDEX 20, France.

PMID: 10089441
DOI: 10.1107/S0907444998008920

Abstract

For the first time, crystals of a pyruvate-ferredoxin oxidoreductase (PFOR) suitable for X-ray analysis have been obtained. This enzyme catalyzes, in anaerobic organisms, the crucial energy-yielding reaction of pyruvate decarboxylation to acetylCoA. Polyethylene glycol and divalent metal cations have been used to crystallize the PFOR from the sulfate-reducing bacterium Desulfovibrio africanus. Two different orthorhombic (P212121 ) crystal forms have been grown with unit-cell dimensions a = 86.1, b = 146.7, c = 212.5 A and a = 84.8, b = 144.9, c = 203.0 A. Both crystals diffract to 2.3 A resolution using synchrotron radiation.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Crystallization
Crystallography, X-Ray
Desulfovibrio / enzymology*
Energy Metabolism
Ketone Oxidoreductases / chemistry*
Ketone Oxidoreductases / isolation & purification*
Ketone Oxidoreductases / metabolism
Pyruvate Synthase

Substances

Ketone Oxidoreductases
Pyruvate Synthase