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Tartryl-CoA inhibits succinyl-CoA synthetase.

Ji HuangMarie E Fraser
Published in: Acta crystallographica. Section F, Structural biology communications (2020)
Succinyl-CoA synthetase (SCS) catalyzes the only substrate-level phosphorylation step in the tricarboxylic acid cycle. Human GTP-specific SCS (GTPSCS), an αβ-heterodimer, was produced in Escherichia coli. The purified protein crystallized from a solution containing tartrate, CoA and magnesium chloride, and a crystal diffracted to 1.52 Å resolution. Tartryl-CoA was discovered to be bound to GTPSCS. The CoA portion lies in the amino-terminal domain of the α-subunit and the tartryl end extends towards the catalytic histidine residue. The terminal carboxylate binds to the phosphate-binding site of GTPSCS.
Keyphrases
  • fatty acid
  • escherichia coli
  • amino acid
  • small molecule
  • staphylococcus aureus
  • protein kinase
  • protein protein
  • crystal structure
  • solid state