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

From National Research Council Canada

DOIResolve DOI: https://doi.org/10.1074/jbc.M510522200
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Name affiliation
  1. National Research Council Canada. NRC Biotechnology Research Institute
FormatText
TypeArticle
Journal titleThe Journal of Biological Chemistry
ISSN0021-9258
1083-351X
Volume280
Issue52
Pages42919–42928
Subjectbacteria; crystal structure; Escherichia coli; in vitro; pharmaceutical; protein; substrate specificity
Abstract
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
Publication date
PublisherAmerican Society for Biochemistry and Molecular Biology
LanguageEnglish
Peer reviewedYes
NRC numberNRC-BRI-47494
NPARC number3538919
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Record identifier04d7f176-35ed-4aad-a78f-da35967bc320
Record created2009-03-01
Record modified2020-02-19
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