6wcv
From Proteopedia
Tartryl-CoA bound to human GTP-specific succinyl-CoA synthetase
Structural highlights
DiseaseSUCA_HUMAN Fatal infantile lactic acidosis with methylmalonic aciduria. The disease is caused by mutations affecting the gene represented in this entry. FunctionSUCA_HUMAN Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and specificity for either ATP or GTP is provided by different beta subunits.[HAMAP-Rule:MF_03222] Publication Abstract from PubMedSuccinyl-CoA synthetase (SCS) catalyzes the only substrate-level phosphorylation step in the tricarboxylic acid cycle. Human GTP-specific SCS (GTPSCS), an alphabeta-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 A resolution. Tartryl-CoA was discovered to be bound to GTPSCS. The CoA portion lies in the amino-terminal domain of the alpha-subunit and the tartryl end extends towards the catalytic histidine residue. The terminal carboxylate binds to the phosphate-binding site of GTPSCS. Tartryl-CoA inhibits succinyl-CoA synthetase.,Huang J, Fraser ME Acta Crystallogr F Struct Biol Commun. 2020 Jul 1;76(Pt 7):302-308. doi: , 10.1107/S2053230X20008201. Epub 2020 Jul 1. PMID:32627745[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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