来自非洲脱硫弧菌的丙酮酸-铁氧化还原蛋白氧化还原酶的结晶及初步晶体学分析。

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

作者信息

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

机构信息

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

出版信息

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

DOI:10.1107/S0907444998008920

PMID:10089441

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.

摘要

首次获得了适合进行X射线分析的丙酮酸-铁氧还蛋白氧化还原酶（PFOR）晶体。这种酶在厌氧生物中催化丙酮酸脱羧生成乙酰辅酶A这一关键的能量产生反应。已使用聚乙二醇和二价金属阳离子使来自非洲脱硫弧菌这种硫酸盐还原菌的PFOR结晶。已培养出两种不同的正交晶系（P212121）晶体形式，其晶胞参数为a = 86.1、b = 146.7、c = 212.5 Å以及a = 84.8、b = 144.9、c = 203.0 Å。使用同步辐射时，两种晶体的衍射分辨率均达到2.3 Å。