Open AccessExpression, purification and preliminary crystallographic analysis of N ‐acetylglucosamine‐1‐phosphate uridylyltransferase from Mycobacterium tuberculosis
Author(s) -
Yin Jiang,
Garen Craig R.,
Cherney Maia M.,
Cherney Leonid T.,
James Michael N. G.
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108024500
Subject(s) - mycobacterium tuberculosis , microbiology and biotechnology , tuberculosis , phosphate , chemistry , mycobacterium , biology , biochemistry , medicine , pathology
The gene product of open reading frame Rv1018c from Mycobacterium tuberculosis is annotated as encoding a probable N ‐acetylglucosamine 1‐phosphate uridylyltransferase ( Mtb GlmU), 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 R 32 and processed to a resolution of 2.2 Å.