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

页码：805 / 808

页数：4

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