3t5c

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Template:STRUCTURE 3t5c

Contents

Crystal structure of N-terminal domain of FACL13 from Mycobacterium tuberculosis in different space group C2

Template:ABSTRACT PUBMED 22206988

Function

[FAC13_MYCTU] Required for maintaining the appropriate mycolic acid composition and permeability of the envelope on its exposure to acidic pH. Catalyzes the activation of long-chain fatty acids as acyl-coenzyme A (acyl-CoA), which are then transferred to the multifunctional polyketide synthase (PKS) type III for further chain extension. It has preference for the fatty acid with long chain length in the following order: hexacosanoic acid (C26), tetracosanoic acid (C24) and palmitic acid (C16).[1] [2] [3]

About this Structure

3t5c is a 2 chain structure with sequence from Mycobacterium tuberculosis h37rv. Full crystallographic information is available from OCA.

Reference

  • Goyal A, Verma P, Anandhakrishnan M, Gokhale RS, Sankaranarayanan R. Molecular Basis of the Functional Divergence of Fatty Acyl-AMP Ligase Biosynthetic Enzymes of Mycobacterium tuberculosis. J Mol Biol. 2011 Dec 21. PMID:22206988 doi:10.1016/j.jmb.2011.12.031
  1. ↑ Singh A, Gupta R, Vishwakarma RA, Narayanan PR, Paramasivan CN, Ramanathan VD, Tyagi AK. Requirement of the mymA operon for appropriate cell wall ultrastructure and persistence of Mycobacterium tuberculosis in the spleens of guinea pigs. J Bacteriol. 2005 Jun;187(12):4173-86. PMID:15937179 doi:10.1128/JB.187.12.4173-4186.2005
  2. ↑ Khare G, Gupta V, Gupta RK, Gupta R, Bhat R, Tyagi AK. Dissecting the role of critical residues and substrate preference of a Fatty Acyl-CoA Synthetase (FadD13) of Mycobacterium tuberculosis. PLoS One. 2009 Dec 21;4(12):e8387. doi: 10.1371/journal.pone.0008387. PMID:20027301 doi:10.1371/journal.pone.0008387
  3. ↑ Andersson CS, Lundgren CA, Magnusdottir A, Ge C, Wieslander A, Molina DM, Hogbom M. The Mycobacterium tuberculosis Very-Long-Chain Fatty Acyl-CoA Synthetase: Structural Basis for Housing Lipid Substrates Longer than the Enzyme. Structure. 2012 May 2. PMID:22560731 doi:10.1016/j.str.2012.03.012

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