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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Crystallization and preliminary X-ray crystallographic analysis of malonyl-CoA decarboxylase from Rhizobium leguminosarum bv. trifolii.
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Crystallization and preliminary X-ray crystallographic analysis of malonyl-CoA decarboxylase from Rhizobium leguminosarum bv. trifolii.

机译：结晶和初步的x射线晶体分析malonyl-CoA脱羧酶从根瘤菌leguminosarum bv。

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摘要

Malonyl-CoA decarboxylase (MCD), which catalyzes the conversion of malonyl-CoA to acetyl-CoA, is an evolutionarily distinct and highly conserved enzyme. MCD does not share sequence homology with other known decarboxylases, while the enzymes from different species exhibit at least >30% sequence identity to each other. In order to provide a canonical structure of the enzyme for detailed study of its structure-function relationship, the MCD of Rhizobium leguminosarum bv. trifolii was overexpressed and crystallized. The crystals belong to the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 133.45, b = 127.10, c = 66.37 A. The asymmetric unit is likely to contain two molecules of MCD (molecular weight of 51 418 Da), with a crystal Volume per protein weight (V(M)) of 2.69 A(3) Da(-1) and a solvent content of about 54.3% by Volume. A native data set to 3.0 A resolution was obtained using a rotating-anode X-ray generator.
机译：Malonyl-CoA脱羧酶(MCD)催化malonyl-CoA乙酰辅酶a,转换在进化上是截然不同的和高度保守的酶。其他已知的脱羧酶,酶从不同物种表现出至少> 30%序列的身份。提供一个规范化的酶的结构详细研究其结构关系,根瘤菌的MCD leguminosarumbv。晶体属斜方晶系的空间集团P2(1) 2(1) 2,晶胞参数=133.45, b = 127.10, c = 66.37。单位可能包含两个分子51(分子量418 Da),水晶体积每蛋白质重量(V (M)) 2.69 (3)Da(1)和溶剂含量约54.3%体积。获得使用一个旋转阳极x射线发生器。

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