Structure of GTP-specific succinyl-CoA synthetase in complex with CoA

Acta Crystallogr F Struct Biol Commun. 2015 Aug;71(Pt 8):1067-71. doi: 10.1107/S2053230X15011188. Epub 2015 Jul 29.

Abstract

Pig GTP-specific succinyl-CoA synthetase is an αβ-heterodimer. The crystal structure of the complex with the substrate CoA was determined at 2.1 Å resolution. The structure shows CoA bound to the amino-terminal domain of the α-subunit, with the free thiol extending from the adenine portion into the site where the catalytic histidine residue resides.

Keywords: ATP-grasp fold; ligase.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acyl Coenzyme A / chemistry*
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Binding Sites
  • Cloning, Molecular
  • Crystallization
  • Crystallography, X-Ray
  • Escherichia coli / genetics
  • Escherichia coli / metabolism
  • Gene Expression
  • Guanosine Triphosphate / chemistry*
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Binding
  • Protein Folding
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Protein Subunits / chemistry*
  • Protein Subunits / genetics
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Sequence Alignment
  • Succinate-CoA Ligases / chemistry*
  • Succinate-CoA Ligases / genetics
  • Swine

Substances

  • Acyl Coenzyme A
  • Protein Subunits
  • Recombinant Proteins
  • Guanosine Triphosphate
  • succinyl-coenzyme A
  • Succinate-CoA Ligases

Associated data

  • PDB/4XX0