Expression, purification and preliminary crystallographic analysis of N-acetylglucosamine-1-phosphate uridylyltransferase from Mycobacterium tuberculosis

被引：3
|
作者：
Yin, Jiang [1 ]
Garen, Craig R. [1 ]
Cherney, Maia M. [1 ]
Cherney, Leonid T. [1 ]
James, Michael N. G. [1 ]
机构：
[1] Univ Alberta, Dept Biochem, Prot Struct & Funct Grp, Edmonton, AB T6G 2H7, Canada
来源：
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2008年 / 64卷
关键词：
D O I：
10.1107/S1744309108024500
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
The gene product of open reading frame Rv1018c from Mycobacterium tuberculosis is annotated as encoding a probable N-acetylglucosamine 1-phosphate uridylyltransferase (MtbGlmU), an enzyme that catalyzes the biosynthesis of UDP-N-acetylglucosamine, a precursor common to lipopolysaccharide and peptidoglycan biosynthesis. Following overexpression in Escherichia coli, the enzyme was purified and crystallized using the hanging-drop vapour-diffusion method. Native diffraction data were collected from crystals belonging to space group R32 and processed to a resolution of 2.2 angstrom.
引用
收藏
页码：805 / 808
页数：4
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