大肠杆菌中二氨基庚二酸差向异构酶的结晶及初步X射线衍射分析
Crystallization and preliminary X-ray diffraction analysis of diaminopimelate epimerase from Escherichia coli.
作者信息
Hor Lilian, Dobson Renwick C J, Dogovski Con, Hutton Craig A, Perugini Matthew A
机构信息
School of Chemistry, The University of Melbourne, Parkville, Victoria 3010, Australia.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Jan 1;66(Pt 1):37-40. doi: 10.1107/S1744309109047708. Epub 2009 Dec 25.
Abstract
Diaminopimelate (DAP) epimerase (EC 5.1.1.7) catalyzes the penultimate step of lysine biosynthesis in bacteria and plants, converting L,L-diaminopimelate to meso-diaminopimelate. Here, the cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of DAP epimerase from Escherichia coli are presented. Crystals were obtained in space group P4(1)2(1)2 and diffracted to 2.0 A resolution, with unit-cell parameters a = b = 89.4, c = 179.6 A. Molecular replacement was conducted using Bacillus anthracis DAP epimerase as a search model and showed the presence of two molecules in the asymmetric unit, with an initial R(free) of 0.456 and R(work) of 0.416.
摘要
二氨基庚二酸（DAP）差向异构酶（EC 5.1.1.7）催化细菌和植物中赖氨酸生物合成的倒数第二步反应，将L，L-二氨基庚二酸转化为内消旋二氨基庚二酸。本文介绍了来自大肠杆菌的DAP差向异构酶的克隆、表达、纯化、结晶及初步X射线衍射分析。晶体属于P4(1)2(1)2空间群，衍射分辨率达到2.0 Å，晶胞参数a = b = 89.4，c = 179.6 Å。以炭疽芽孢杆菌DAP差向异构酶作为搜索模型进行分子置换，结果表明不对称单元中有两个分子，初始R（自由）值为0.456，R（工作）值为0.416。
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