4xx0
From Proteopedia
(Difference between revisions)
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/SUCA_PIG SUCA_PIG]] Catalyzes the ATP- or GTP-dependent ligation of succinate and CoA to form succinyl-CoA. The nature of the beta subunit determines the nucleotide specificity (By similarity). [[http://www.uniprot.org/uniprot/SUCB2_PIG SUCB2_PIG]] Catalyzes the GTP-dependent ligation of succinate and CoA to form succinyl-CoA (By similarity). | [[http://www.uniprot.org/uniprot/SUCA_PIG SUCA_PIG]] Catalyzes the ATP- or GTP-dependent ligation of succinate and CoA to form succinyl-CoA. The nature of the beta subunit determines the nucleotide specificity (By similarity). [[http://www.uniprot.org/uniprot/SUCB2_PIG SUCB2_PIG]] Catalyzes the GTP-dependent ligation of succinate and CoA to form succinyl-CoA (By similarity). | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Pig GTP-specific succinyl-CoA synthetase is an alphabeta-heterodimer. The crystal structure of the complex with the substrate CoA was determined at 2.1 A resolution. The structure shows CoA bound to the amino-terminal domain of the alpha-subunit, with the free thiol extending from the adenine portion into the site where the catalytic histidine residue resides. | ||
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| + | Structure of GTP-specific succinyl-CoA synthetase in complex with CoA.,Huang J, Malhi M, Deneke J, Fraser ME Acta Crystallogr F Struct Biol Commun. 2015 Aug 1;71(Pt 8):1067-71. doi:, 10.1107/S2053230X15011188. Epub 2015 Jul 29. PMID:26249701<ref>PMID:26249701</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 07:45, 26 August 2015
CoA bound to pig GTP-specific succinyl-CoA synthetase
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