发酵乳杆菌谷氨酸消旋酶的结晶及初步X射线晶体学研究。
Crystallization and preliminary X-ray crystallographic studies of glutamate racemase from Lactobacillus fermenti.
作者信息
Lee Ki-Seog, Park Seon-Mi, Hwang Kwang Yeon, Chi Young-Min
机构信息
Division of Biotechnology and Genetic Engineering, Korea University, Seoul 136-701, South Korea.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Feb 1;61(Pt 2):199-201. doi: 10.1107/S1744309104034426. Epub 2005 Jan 20.
Glutamate racemase catalyzes the conversion of L-glutamic acid to D-glutamic acid and vice versa. Since D-glutamic acid is one of the essential amino acids present in peptidoglycan, glutamate racemase has been considered to be an attractive target for the design of new antibacterial drugs. Glutamate racemase from Lactobacillus fermenti has been crystallized by the hanging-drop vapour-diffusion method using polyethylene glycol 8000 as a precipitant. The crystals belong to the orthorhombic space group C222(1), with unit-cell parameters a = 98.32, b = 184.09, c = 45.99 A. The asymmetric unit contains one molecule, corresponding to a VM value of 1.84 A3 Da(-1). A complete data set has been collected from the native enzyme at 2.28 A resolution using a synchrotron-radiation source.
谷氨酸消旋酶催化L-谷氨酸与D-谷氨酸之间的相互转化。由于D-谷氨酸是肽聚糖中存在的必需氨基酸之一，谷氨酸消旋酶被认为是新型抗菌药物设计的一个有吸引力的靶点。来自发酵乳杆菌的谷氨酸消旋酶已通过悬滴气相扩散法，以聚乙二醇8000作为沉淀剂进行了结晶。晶体属于正交晶系空间群C222(1)，晶胞参数a = 98.32，b = 184.09，c = 45.99 Å。不对称单元包含一个分子，对应于1.84 ų Da⁻¹的VM值。使用同步辐射源在2.28 Å分辨率下从天然酶收集了完整的数据集。
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