Open AccessExpression, purification and preliminary crystallographic analysis of O ‐acetylhomoserine sulfhydrylase from Mycobacterium tuberculosis
Author(s) -
Yin Jiang,
Garen Craig R.,
Bateman Katherine,
Yu Minmin,
Alipio Lyon Emily Z.,
Habel Jeff,
Kim Heungbok,
Hung Liwei,
Kim ChangYub,
James Michael N. G.
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111017611
Subject(s) - mycobacterium tuberculosis , escherichia coli , open reading frame , methionine , chemistry , resolution (logic) , enzyme , amino acid , biochemistry , biosynthesis , tuberculosis , gene , peptide sequence , medicine , pathology , artificial intelligence , computer science
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 P 2 1 and were processed to a resolution of 2.1 Å.