3t5a

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Template:STRUCTURE 3t5a

Contents

Crystal structure of N-terminal domain of FAAL28 G330W mutant from Mycobacterium tuberculosis

Template:ABSTRACT PUBMED 22206988

Function

[FAA28_MYCTU] Catalyzes the activation of long-chain fatty acids (C22-24 fatty acids) as acyl-adenylates (acyl-AMP), which are then transferred to the multifunctional polyketide synthase Mas for further chain extension. Involved in the biosynthesis of mycoserates.[1] [2] [3]

About this Structure

3t5a is a 1 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. ↑ Cox JS, Chen B, McNeil M, Jacobs WR Jr. Complex lipid determines tissue-specific replication of Mycobacterium tuberculosis in mice. Nature. 1999 Nov 4;402(6757):79-83. PMID:10573420 doi:10.1038/47042
  2. ↑ Camacho LR, Constant P, Raynaud C, Laneelle MA, Triccas JA, Gicquel B, Daffe M, Guilhot C. Analysis of the phthiocerol dimycocerosate locus of Mycobacterium tuberculosis. Evidence that this lipid is involved in the cell wall permeability barrier. J Biol Chem. 2001 Jun 8;276(23):19845-54. Epub 2001 Mar 13. PMID:11279114 doi:10.1074/jbc.M100662200
  3. ↑ Trivedi OA, Arora P, Sridharan V, Tickoo R, Mohanty D, Gokhale RS. Enzymic activation and transfer of fatty acids as acyl-adenylates in mycobacteria. Nature. 2004 Mar 25;428(6981):441-5. PMID:15042094 doi:10.1038/nature02384

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