Crystallization and X-ray diffraction analysis of peroxisomal Delta3-Delta2-enoyl-CoA isomerase from Saccharomyces cerevisiae

Acta Crystallogr D Biol Crystallogr. 2000 Aug;56(Pt 8):1020-3. doi: 10.1107/s0907444900006533.

Abstract

The purification, crystallization and X-ray diffraction analysis of Saccharomyces cerevisiae Delta(3)-Delta(2)-enoyl-CoA isomerase is described. Delta(3)-Delta(2)-Enoyl-CoA isomerase is a member of the hydratase/isomerase protein family and is an auxiliary enzyme required for the beta-oxidation of unsaturated fatty acids. It is a hexameric enzyme consisting of six identical 32 kDa subunits of 280 residues each. In crystallization trials three crystal forms were obtained, with tetragonal and hexagonal lattices. A 2.5 A data set was collected from the unliganded hexagonal crystals with an R(merge) of 6.6%. The crystal, with unit-cell parameters a = 116.0, b = 116.0, c = 122.9 A, is likely to have P6(3)22 symmetry.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Carbon-Carbon Double Bond Isomerases / chemistry*
  • Carbon-Carbon Double Bond Isomerases / genetics
  • Carbon-Carbon Double Bond Isomerases / isolation & purification
  • Crystallization
  • Crystallography, X-Ray
  • Dodecenoyl-CoA Isomerase
  • Escherichia coli / genetics
  • Molecular Weight
  • Peroxisomes / enzymology
  • Protein Structure, Quaternary
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Recombinant Proteins / isolation & purification
  • Saccharomyces cerevisiae / enzymology*

Substances

  • Recombinant Proteins
  • Carbon-Carbon Double Bond Isomerases
  • Dodecenoyl-CoA Isomerase