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Tartryl‐CoA inhibits succinyl‐CoA synthetase
Author(s) -
Huang Ji,
Fraser Marie E.
Publication year - 2020
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x20008201
Subject(s) - chemistry , residue (chemistry) , protein subunit , biochemistry , histidine , gtp' , citric acid cycle , coenzyme a , carboxylate , stereochemistry , enzyme , reductase , gene
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.