Open AccessExpression, purification and preliminary crystallographic analysis of Rv2247, the β subunit of acyl‐CoA carboxylase (ACCD6) from Mycobacterium tuberculosis
Author(s) -
Niu Chunying,
Yin Jiang,
Cherney Maia M.,
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/s1744309111038413
Subject(s) - mycobacterium tuberculosis , pyruvate carboxylase , acetyl coa carboxylase , protein subunit , biosynthesis , chemistry , biochemistry , biology , tuberculosis , crystallography , microbiology and biotechnology , enzyme , gene , medicine , pathology
Mycobacterium tuberculosis ( Mtb ) acyl‐CoA carboxylase is involved in the biosynthesis of mycolic acids, which are a key component of the bacillus cell wall. The Mtb genome encodes six acyl‐CoA carboxylase β subunits (ACCD1–6), three of which (ACCD4–6) are essential for survival of the pathogen on minimal medium. Mtb ACCD6 has been expressed, purified and crystallized. The two forms of Mtb ACCD6 crystals belonged to space groups P 4 1 2 1 2 and P 2 1 2 1 2 1 and diffracted to 2.9 and 2.5 Å resolution, respectively, at a synchrotron‐radiation source.