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结核分枝杆菌O-乙酰高丝氨酸巯基化酶的表达、纯化及初步晶体学分析

Expression, purification and preliminary crystallographic analysis of O-acetylhomoserine sulfhydrylase from Mycobacterium tuberculosis.

作者信息

Yin Jiang, Garen Craig R, Bateman Katherine, Yu Minmin, Lyon Emily Z Alipio, Habel Jeff, Kim Heungbok, Hung Li-wei, Kim Chang-Yub, James Michael N G

机构信息

Department of Biochemistry, School of Molecular and Systems Medicine, Faculty of Medicine and Dentistry, University of Alberta, Edmonton, Alberta, Canada.

出版信息

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Aug 1;67(Pt 8):959-63. doi: 10.1107/S1744309111017611. Epub 2011 Jul 27.

DOI:10.1107/S1744309111017611
PMID:21821905
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3151138/
Abstract

The gene product of the open reading frame Rv3340 from Mycobacterium tuberculosis is annotated as encoding a probable O-acetylhomoserine (OAH) sulfhydrylase (MetC), an enzyme that catalyzes the last step in the biosynthesis of methionine, which is an essential amino acid in bacteria and plants. Following overexpression in Escherichia coli, the M. tuberculosis MetC enzyme was purified and crystallized using the hanging-drop vapor-diffusion method. Native diffraction data were collected from crystals belonging to space group P2(1) and were processed to a resolution of 2.1 Å.

摘要

结核分枝杆菌开放阅读框Rv3340的基因产物被注释为编码一种可能的O-乙酰高丝氨酸（OAH）巯基化酶（MetC），该酶催化甲硫氨酸生物合成的最后一步，甲硫氨酸是细菌和植物中的必需氨基酸。在大肠杆菌中过表达后，结核分枝杆菌MetC酶通过悬滴气相扩散法进行纯化和结晶。从属于空间群P2(1)的晶体收集原生衍射数据，并将其处理至2.1 Å的分辨率。

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