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Structure of GTP‐specific succinyl‐CoA synthetase in complex with CoA
Author(s) -
Huang Ji,
Malhi Manpreet,
Deneke Jan,
Fraser Marie Elizabeth
Publication year - 2015
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/s2053230x15011188
Subject(s) - gtp' , chemistry , histidine , residue (chemistry) , protein subunit , stereochemistry , biochemistry , binding site , c terminus , amino acid , enzyme , gene
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.