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首页> 外文期刊>Acta crystallographica, Section F. Structural biology and crystallization communications >Expression, crystallization and preliminary X-ray crystallographic analysis of alanine racemase from Acinetobacter baumannii OXA-23
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Expression, crystallization and preliminary X-ray crystallographic analysis of alanine racemase from Acinetobacter baumannii OXA-23

机译：鲍曼不动杆菌OXA-23中丙氨酸消旋酶的表达，结晶及初步X射线晶体学分析

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摘要

Acinetobacter baumannii has received much attention owing to its exceptional ability to develop resistance to currently available antibiotics. Alanine racemase (ALR) catalyzes the racemization of l-alanine to D-alanine with pyridoxal 5'-phosphate (PLP) as a cofactor. The d-alanine product is an essential component of the bacterial cell wall and ALR is a potential target for the development of novel antibacterial drugs. The alr gene from A. baumannii was cloned and the protein (AbALR) was expressed, purified and crystallized. The AbALR crystal diffracted to 2.3 angstrom resolution and belonged to the primitive orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 55.1, b = 85.0, c = 167.7 angstrom. Two protomers were present in the asymmetric unit, with a corresponding V-M value of 2.3 angstrom(3) Da(-1) and a solvent content of 47.5%.
机译：鲍曼不动杆菌由于其对目前可获得的抗生素产生抗药性的卓越能力而备受关注。丙氨酸消旋酶（ALR）以吡ido醛5'-磷酸（PLP）作为辅因子催化1-丙氨酸向D-丙氨酸的消旋。 d-丙氨酸产物是细菌细胞壁的重要组成部分，ALR是开发新型抗菌药物的潜在靶标。克隆了鲍曼不动杆菌的alr基因，并表达，纯化和结晶了蛋白质（AbALR）。 AbALR晶体衍射到2.3埃分辨率，并属于原始正交晶空间群P2（1）2（1）2（1），单位晶胞参数a = 55.1，b = 85.0，c = 167.7埃。在不对称单元中存在两个protomer，相应的V-M值为2.3埃（3）Da（-1），溶剂含量为47.5％。

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