1. Academic Validation
  2. Tartryl-CoA inhibits succinyl-CoA synthetase

Tartryl-CoA inhibits succinyl-CoA synthetase

  • Acta Crystallogr F Struct Biol Commun. 2020 Jul 1;76(Pt 7):302-308. doi: 10.1107/S2053230X20008201.
Ji Huang 1 Marie E Fraser 1
Affiliations

Affiliation

  • 1 Department of Biological Sciences, University of Calgary, 2500 University Drive NW, Calgary, Alberta T2N 1N4, Canada.
Abstract

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.

Keywords

catalysis; succinyl-CoA synthetase; thioesters; tricarboxylic acid cycle.

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