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

Autor:	Manpreet Malhi, Jan Deneke, Ji Huang, Marie E. Fraser
Rok vydání:	2015
Předmět:	Models Molecular Protein Folding GTP' Swine Molecular Sequence Data Biophysics Gene Expression Biology Guanosine triphosphate Crystallography X-Ray Biochemistry Protein Structure Secondary Research Communications chemistry.chemical_compound Structural Biology Succinate-CoA Ligases Genetics Escherichia coli Animals Amino Acid Sequence Binding site Cloning Molecular chemistry.chemical_classification DNA ligase Binding Sites Base Sequence Succinyl coenzyme A synthetase organic chemicals Substrate (chemistry) Condensed Matter Physics Recombinant Proteins Protein Structure Tertiary Protein Subunits chemistry bacteria Protein folding Acyl Coenzyme A Guanosine Triphosphate Crystallization Sequence Alignment Protein Binding
Zdroj:	Acta crystallographica. Section F, Structural biology communications. 71(Pt 8)
ISSN:	2053-230X
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a7fe84719e3b516041abc60b559c882e https://pubmed.ncbi.nlm.nih.gov/26249701 Zobrazit plný text záznamu Plný text ve formátu PDF