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Article Dans Une Revue Acta crystallographica Section F : Structural biology communications [2014-...] Année : 2007

Structure of Mycobacterium tuberculosis mtFabD, a malonyl-CoA:acyl carrier protein transacylase (MCAT).

Hemza Ghadbane
  • Fonction : Auteur
Gurdyal S Besra
  • Fonction : Auteur
Klaus Fütterer
  • Fonction : Auteur

Résumé

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.

Dates et versions

hal-00203080 , version 1 (08-01-2008)

Identifiants

Citer

Hemza Ghadbane, Alistair K Brown, Laurent Kremer, Gurdyal S Besra, Klaus Fütterer. Structure of Mycobacterium tuberculosis mtFabD, a malonyl-CoA:acyl carrier protein transacylase (MCAT).. Acta crystallographica Section F : Structural biology communications [2014-..], 2007, 63 (Pt 10), pp.831-5. ⟨10.1107/S1744309107042455⟩. ⟨hal-00203080⟩
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