1KAS
BETA-KETOACYL-ACP SYNTHASE II FROM ESCHERICHIA COLI
Summary for 1KAS
| Entry DOI | 10.2210/pdb1kas/pdb |
| Descriptor | BETA-KETOACYL ACP SYNTHASE II (2 entities in total) |
| Functional Keywords | acyltransferase, condensing enzyme, fatty acid elongation, lipid metabolism, alpha-beta protein, five-layered fold, alpha-beta-alpha-beta-alpha |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 42958.43 |
| Authors | Huang, W.,Jia, J.,Edwards, P.,Dehesh, K.,Schneider, G.,Lindqvist, Y. (deposition date: 1997-12-22, release date: 1999-03-02, Last modification date: 2024-02-07) |
| Primary citation | Huang, W.,Jia, J.,Edwards, P.,Dehesh, K.,Schneider, G.,Lindqvist, Y. Crystal structure of beta-ketoacyl-acyl carrier protein synthase II from E.coli reveals the molecular architecture of condensing enzymes. EMBO J., 17:1183-1191, 1998 Cited by PubMed Abstract: In the biosynthesis of fatty acids, the beta-ketoacyl-acyl carrier protein (ACP) synthases catalyze chain elongation by the addition of two-carbon units derived from malonyl-ACP to an acyl group bound to either ACP or CoA. The crystal structure of beta-ketoacyl synthase II from Escherichia coli has been determined with the multiple isomorphous replacement method and refined at 2.4 A resolution. The subunit consists of two mixed five-stranded beta-sheets surrounded by alpha-helices. The two sheets are packed against each other in such a way that the fold can be described as consisting of five layers, alpha-beta-alpha-beta-alpha. The enzyme is a homodimer, and the subunits are related by a crystallographic 2-fold axis. The two active sites are located near the dimer interface but are approximately 25 A apart. The proposed nucleophile in the reaction, Cys163, is located at the bottom of a mainly hydrophobic pocket which is also lined with several conserved polar residues. In spite of very low overall sequence homology, the structure of beta-ketoacyl synthase is similar to that of thiolase, an enzyme involved in the beta-oxidation pathway, indicating that both enzymes might have a common ancestor. PubMed: 9482715DOI: 10.1093/emboj/17.5.1183 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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