The X-ray crystal structure of beta-ketoacyl [acyl carrier protein] synthase I

FEBS Lett. 1999 Oct 22;460(1):46-52. doi: 10.1016/s0014-5793(99)01303-4.

Abstract

The crystal structure of the fatty acid elongating enzyme beta-ketoacyl [acyl carrier protein] synthase I (KAS I) from Escherichia coli has been determined to 2.3 A resolution by molecular replacement using the recently solved crystal structure of KAS II as a search model. The crystal contains two independent dimers in the asymmetric unit. KAS I assumes the thiolase alpha(beta)alpha(beta)alpha fold. Electrostatic potential distribution reveals an acyl carrier protein docking site and a presumed substrate binding pocket was detected extending the active site. Both subunits contribute to each substrate binding site in the dimer.

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Crystallography, X-Ray
  • Dimerization
  • Escherichia coli
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Conformation
  • Protein Structure, Secondary
  • Recombinant Proteins / chemistry
  • Sequence Alignment
  • Static Electricity
  • Transferases (Other Substituted Phosphate Groups) / chemistry*

Substances

  • Recombinant Proteins
  • Transferases (Other Substituted Phosphate Groups)
  • holo-(acyl-carrier-protein) synthase