2qj3
From Proteopedia
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Mycobacterium tuberculosis FabD
Overview
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 A resolution by multi-wavelength anomalous dispersion. Phasing was facilitated by Ni2+ ions bound to the 20-residue N-terminal affinity tag, which packed between the two independent copies of mtFabD.
About this Structure
2QJ3 is a Single protein structure of sequence from Mycobacterium tuberculosis with as ligand. Active as [Acyl-carrier-protein_S-malonyltransferase [Acyl-carrier-protein] S-malonyltransferase], with EC number 2.3.1.39 Full crystallographic information is available from OCA.
Reference
Structure of Mycobacterium tuberculosis mtFabD, a malonyl-CoA:acyl carrier protein transacylase (MCAT)., Ghadbane H, Brown AK, Kremer L, Besra GS, Futterer K, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Oct 1;63(Pt, 10):831-5. Epub 2007 Sep 19. PMID:17909282[[Category: [Acyl-carrier-protein] S-malonyltransferase]]
Page seeded by OCA on Thu Feb 21 18:39:50 2008
