来自假单胞菌属RS-16菌株的羧肽酶G2的结晶及初步晶体学分析

Crystallization and preliminary crystallographic analysis of carboxypeptidase G2 from Pseudomonas sp. strain RS-16.

作者信息

Lloyd L F, Collyer C A, Sherwood R F

机构信息

Blackett Laboratory, Imperial College, London, U.K.

出版信息

J Mol Biol. 1991 Jul 5;220(1):17-8. doi: 10.1016/0022-2836(91)90377-i.

DOI:10.1016/0022-2836(91)90377-i

PMID:2067015

Abstract

Carboxypeptidase G2, a zinc metalloenzyme isolated from Pseudomonas sp. strain RS-16, which catalyses the hydrolytic cleavage of reduced and non-reduced folates to pteroates and L-glutamate, has been crystallized from polyethylene glycol (average Mr 4000) by vapour diffusion. The crystal symmetry is monoclinic C2, with unit cell dimensions a = 206 A, b = 82 A, c = 116 A and beta = 118 degrees. The molecular mass and volume of the unit cell suggest that there are two dimers of the enzyme in the asymmetric unit. The crystals diffract to at least 3.0 A and are suitable for X-ray structure analysis.

摘要

羧肽酶G2是一种从假单胞菌属RS-16菌株中分离出的锌金属酶，它催化还原型和非还原型叶酸水解裂解为蝶酸和L-谷氨酸，已通过气相扩散法从聚乙二醇（平均分子量4000）中结晶出来。晶体对称性为单斜晶系C2，晶胞参数a = 206 Å，b = 82 Å，c = 116 Å，β = 118°。晶胞的分子量和体积表明，不对称单元中有两个酶二聚体。这些晶体的衍射分辨率至少为3.0 Å，适合进行X射线结构分析。