Open AccessStructure of Mycobacterium tuberculosis mtFabD, a malonyl‐CoA:acyl carrier protein transacylase (MCAT)
Author(s) -
Ghadbane Hemza,
Brown Alistair K.,
Kremer Laurent,
Besra Gurdyal S.,
Fütterer Klaus
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107042455
Subject(s) - acyl carrier protein , chemistry , biochemistry , peptidoglycan , mycobacterium tuberculosis , coenzyme a , mycobacterium , stereochemistry , enzyme , biosynthesis , biology , bacteria , tuberculosis , genetics , medicine , pathology , reductase
Mycobacteria display a unique and unusual cell‐wall architecture, central to which is the membrane‐proximal mycolyl‐arabinogalactan‐peptidoglycan core (mAGP). The biosynthesis of mycolic acids, which form the outermost layer of the mAGP core, involves malonyl‐CoA:acyl carrier protein transacylase (MCAT). This essential enzyme catalyses the transfer of malonyl from coenzyme A to acyl carrier protein AcpM, thus feeding these two‐carbon units into the chain‐elongation cycle of the type II fatty‐acid synthase. The crystal structure of M. tuberculosis mtFabD, the mycobacterial MCAT, has been determined to 3.0 Å resolution by multi‐wavelength anomalous dispersion. Phasing was facilitated by Ni 2+ ions bound to the 20‐residue N‐terminal affinity tag, which packed between the two independent copies of mtFabD.