Crystallization and preliminary X-ray diffraction studies of an alpha-methylacyl-CoA racemase from Mycobacterium tuberculosis

Acta Crystallogr D Biol Crystallogr. 2003 Feb;59(Pt 2):353-5. doi: 10.1107/s0907444902020735. Epub 2003 Jan 23.

Abstract

alpha-Methylacyl-CoA racemase is a key enzyme in the metabolism of 2-methyl-branched fatty acids and, in mammals, in the conversion of cholesterol to bile acids. The enzyme from Mycobacterium tuberculosis has been purified to homogeneity and crystallized by the hanging-drop vapour-diffusion method. The crystals of the unliganded racemase belong to space group P6(1)22 or P6(5)22, with unit-cell parameters a = b = 122.0, c = 256.4 A. Data sets were collected at 100 K. The crystals diffract to 2.8 A using synchrotron radiation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Crystallization
  • Crystallography, X-Ray
  • Humans
  • Molecular Sequence Data
  • Mycobacterium tuberculosis / enzymology*
  • Racemases and Epimerases / chemistry*
  • Racemases and Epimerases / metabolism
  • Rats
  • Sequence Homology, Amino Acid
  • Synchrotrons

Substances

  • Racemases and Epimerases
  • alpha-methylacyl-CoA racemase