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http://purl.uniprot.org/citations/16253988http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16253988http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16253988http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/16253988http://www.w3.org/2000/01/rdf-schema#comment"Coenzyme A transferases are involved in a broad range of biochemical processes in both prokaryotes and eukaryotes, and exhibit a diverse range of substrate specificities. The YdiF protein from Escherichia coli O157:H7 is an acyl-CoA transferase of unknown physiological function, and belongs to a large sequence family of CoA transferases, present in bacteria to humans, which utilize oxoacids as acceptors. In vitro measurements showed that YdiF displays enzymatic activity with short-chain acyl-CoAs. The crystal structures of YdiF and its complex with CoA, the first co-crystal structure for any Family I CoA transferase, have been determined and refined at 1.9 and 2.0 A resolution, respectively. YdiF is organized into tetramers, with each monomer having an open alpha/beta structure characteristic of Family I CoA transferases. Co-crystallization of YdiF with a variety of CoA thioesters in the absence of acceptor carboxylic acid resulted in trapping a covalent gamma-glutamyl-CoA thioester intermediate. The CoA binds within a well defined pocket at the N- and C-terminal domain interface, but makes contact only with the C-terminal domain. The structure of the YdiF complex provides a basis for understanding the different catalytic steps in the reaction of Family I CoA transferases."xsd:string
http://purl.uniprot.org/citations/16253988http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m510522200"xsd:string
http://purl.uniprot.org/citations/16253988http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m510522200"xsd:string
http://purl.uniprot.org/citations/16253988http://purl.uniprot.org/core/author"Cygler M."xsd:string
http://purl.uniprot.org/citations/16253988http://purl.uniprot.org/core/author"Cygler M."xsd:string
http://purl.uniprot.org/citations/16253988http://purl.uniprot.org/core/author"Li Y."xsd:string
http://purl.uniprot.org/citations/16253988http://purl.uniprot.org/core/author"Li Y."xsd:string
http://purl.uniprot.org/citations/16253988http://purl.uniprot.org/core/author"Fraser M.E."xsd:string
http://purl.uniprot.org/citations/16253988http://purl.uniprot.org/core/author"Fraser M.E."xsd:string
http://purl.uniprot.org/citations/16253988http://purl.uniprot.org/core/author"Matte A."xsd:string
http://purl.uniprot.org/citations/16253988http://purl.uniprot.org/core/author"Matte A."xsd:string
http://purl.uniprot.org/citations/16253988http://purl.uniprot.org/core/author"Ajamian E."xsd:string
http://purl.uniprot.org/citations/16253988http://purl.uniprot.org/core/author"Ajamian E."xsd:string
http://purl.uniprot.org/citations/16253988http://purl.uniprot.org/core/author"Rangarajan E.S."xsd:string
http://purl.uniprot.org/citations/16253988http://purl.uniprot.org/core/author"Rangarajan E.S."xsd:string
http://purl.uniprot.org/citations/16253988http://purl.uniprot.org/core/author"Iannuzzi P."xsd:string
http://purl.uniprot.org/citations/16253988http://purl.uniprot.org/core/author"Iannuzzi P."xsd:string
http://purl.uniprot.org/citations/16253988http://purl.uniprot.org/core/author"Kernaghan S.D."xsd:string
http://purl.uniprot.org/citations/16253988http://purl.uniprot.org/core/author"Kernaghan S.D."xsd:string
http://purl.uniprot.org/citations/16253988http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/16253988http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/16253988http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string