Crystallographic Trapping of the Glutamyl-CoA Thioester Intermediate of Family I CoA Transferases

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DOIResolve DOI: http://doi.org/10.1074/jbc.M510522200
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TypeArticle
Journal titleJournal of Biological Chemistry
Volume280
Issue52
Pages4291942928; # of pages: 10
SubjectBacteria; crystal structure; Escherichia coli; Human; Humans; I; In Vitro; pha; Protein; Substrate Specificity
AbstractCoenzyme 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
Publication date
AffiliationNRC Biotechnology Research Institute; National Research Council Canada
Peer reviewedNo
NRC number47494
NPARC number3538919
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Record identifier04d7f176-35ed-4aad-a78f-da35967bc320
Record created2009-03-01
Record modified2016-05-09
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