Structure of succinyl-CoA:3-ketoacid CoA transferase from Drosophila melanogaster

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Oct;69(Pt 10):1089-93. doi: 10.1107/S1744309113024986. Epub 2013 Sep 28.

Abstract

Succinyl-CoA:3-ketoacid CoA transferase (SCOT) plays a crucial role in ketone-body metabolism. SCOT from Drosophila melanogaster (DmSCOT) was purified and crystallized. The crystal structure of DmSCOT was determined at 2.64 Å resolution and belonged to space group P212121, with unit-cell parameters a=76.638, b=101.921, c=122.457 Å, α=β=γ=90°. Sequence alignment and structural analysis identified DmSCOT as a class I CoA transferase. Compared with Acetobacter aceti succinyl-CoA:acetate CoA transferase, DmSCOT has a different substrate-binding pocket, which may explain the difference in their substrate specificities.

Keywords: Drosophila melanogaster; class I CoA transferases; succinyl-CoA:3-ketoacid CoA transferase.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Coenzyme A-Transferases / chemistry*
  • Crystallography, X-Ray
  • Drosophila melanogaster / enzymology*
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Multimerization
  • Sequence Alignment
  • Structural Homology, Protein
  • Substrate Specificity

Substances

  • Coenzyme A-Transferases
  • 3-ketoacid CoA-transferase

Associated data

  • PDB/4KGB