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

(2007) Acta Crystallogr Sect F Struct Biol Cryst Commun 63: 831-835

• PubMed: 17909282 Search on PubMedSearch on PubMed Central
• DOI: https://doi.org/10.1107/S1744309107042455
• Primary Citation of Related Structures:  
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• PubMed Abstract: 
  

  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.

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Organizational Affiliation: 

School of Biosciences, The University of Birmingham, Edgbaston, Birmingham B15 2TT, England.