Crystallographic trapping of the glutamyl-CoA thioester intermediate of family I CoA transferases
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 Angstrom 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.
- Research Organization:
- Brookhaven National Laboratory (BNL) National Synchrotron Light Source
- Sponsoring Organization:
- Doe - Office Of Science
- DOE Contract Number:
- AC02-98CH10886
- OSTI ID:
- 913922
- Report Number(s):
- BNL--78490-2007-JA
- Journal Information:
- J. Biol. Chem., Journal Name: J. Biol. Chem. Journal Issue: 52 Vol. 280; ISSN JBCHA3; ISSN 0021-9258
- Country of Publication:
- United States
- Language:
- English
Similar Records
Structural snapshots along the reaction pathway of Yersinia pestis RipA, a putative butyryl-CoA transferase
Functional dissection of the bipartite active site of the class I coenzyme A (CoA)-transferase succinyl-CoA:acetate CoA-transferase
Rapid Biocatalytic Synthesis of Aromatic Acid CoA Thioesters by Using Microbial Aromatic Acid CoA Ligases
Journal Article
·
Tue Apr 01 00:00:00 EDT 2014
· Acta Crystallographica. Section D: Biological Crystallography
·
OSTI ID:22351314
Functional dissection of the bipartite active site of the class I coenzyme A (CoA)-transferase succinyl-CoA:acetate CoA-transferase
Journal Article
·
Sun May 22 20:00:00 EDT 2016
· Frontiers in Chemistry
·
OSTI ID:1345618
Rapid Biocatalytic Synthesis of Aromatic Acid CoA Thioesters by Using Microbial Aromatic Acid CoA Ligases
Journal Article
·
Tue Apr 11 20:00:00 EDT 2023
· ChemBioChem: a European journal of chemical biology
·
OSTI ID:1969598