Crystallization and preliminary X-ray crystallographic studies of fatty acid-CoA racemase from Mycobacterium tuberculosis H37Rv

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Nov 1;61(Pt 11):1017-9. doi: 10.1107/S1744309105034330. Epub 2005 Oct 28.

Abstract

Fatty acid-CoA racemase plays an important role in the beta-oxidation of branched-chain fatty acids and fatty-acid derivatives as it catalyzes the conversion of several (2R)-branched-chain fatty acid-CoAs to their (2S)-stereoisomers. Fatty acid-CoA racemase from Mycobacterium tuberculosis H37Rv has been purified to homogeneity and crystallized by the hanging-drop vapour-diffusion method with polyethylene glycol 4000 as precipitant. The crystals belong to the trigonal space group P3(1) or P3(2), with unit-cell parameters a = b = 109.56, c = 147.97 A. The asymmetric unit contains six monomers, corresponding to a VM value of 2.15 A3 Da(-1). A complete native data set has been collected at 2.7 A resolution using a synchrotron-radiation source.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acyl-CoA Oxidase / chemistry*
  • Acyl-CoA Oxidase / metabolism
  • Crystallization
  • Crystallography, X-Ray
  • Fatty Acids / metabolism
  • Mycobacterium tuberculosis / metabolism
  • Oxygen / metabolism*
  • Polyethylene Glycols / chemistry
  • Protein Conformation
  • Racemases and Epimerases / chemistry*
  • Racemases and Epimerases / metabolism
  • Recombinant Proteins
  • Stereoisomerism
  • Synchrotrons
  • X-Ray Diffraction

Substances

  • Fatty Acids
  • Recombinant Proteins
  • Polyethylene Glycols
  • Acyl-CoA Oxidase
  • Racemases and Epimerases
  • Oxygen