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Structure of GTP-specific succinyl-CoA synthetase in complex with CoA.


ABSTRACT: Pig GTP-specific succinyl-CoA synthetase is an ??-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 ?-subunit, with the free thiol extending from the adenine portion into the site where the catalytic histidine residue resides.

SUBMITTER: Huang J 

PROVIDER: S-EPMC4528943 | biostudies-literature | 2015 Aug

REPOSITORIES: biostudies-literature

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Structure of GTP-specific succinyl-CoA synthetase in complex with CoA.

Huang Ji J   Malhi Manpreet M   Deneke Jan J   Fraser Marie Elizabeth ME  

Acta crystallographica. Section F, Structural biology communications 20150729 Pt 8


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. ...[more]

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