2AHU
Crystal structure of Acyl-CoA transferase (YdiF) apoenzyme from Escherichia coli O157:H7.
Summary for 2AHU
| Entry DOI | 10.2210/pdb2ahu/pdb |
| Related | 2AHV 2AHW |
| Descriptor | putative enzyme ydiF (2 entities in total) |
| Functional Keywords | ydif, coa transferase, glutamyl thioester, structural genomics, montreal-kingston bacterial structural genomics initiative, bsgi, transferase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 4 |
| Total formula weight | 232331.00 |
| Authors | Rangarajan, E.S.,Li, Y.,Ajamian, E.,Iannuzzi, P.,Kernaghan, S.D.,Fraser, M.E.,Cygler, M.,Matte, A.,Montreal-Kingston Bacterial Structural Genomics Initiative (BSGI) (deposition date: 2005-07-28, release date: 2005-11-01, Last modification date: 2024-10-30) |
| Primary citation | Rangarajan, E.S.,Li, Y.,Ajamian, E.,Iannuzzi, P.,Kernaghan, S.D.,Fraser, M.E.,Cygler, M.,Matte, A. Crystallographic trapping of the glutamyl-CoA thioester intermediate of family I CoA transferases. J.Biol.Chem., 280:42919-42928, 2005 Cited by PubMed 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. PubMed: 16253988DOI: 10.1074/jbc.M510522200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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