1kas
From Proteopedia
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'''BETA-KETOACYL-ACP SYNTHASE II FROM ESCHERICHIA COLI''' | '''BETA-KETOACYL-ACP SYNTHASE II FROM ESCHERICHIA COLI''' | ||
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[[Category: Lindqvist, Y.]] | [[Category: Lindqvist, Y.]] | ||
[[Category: Schneider, G.]] | [[Category: Schneider, G.]] | ||
| - | [[Category: | + | [[Category: Acyltransferase]] |
| - | [[Category: | + | [[Category: Alpha-beta protein]] |
| - | [[Category: | + | [[Category: Alpha-beta-alpha-beta-alpha]] |
| - | [[Category: | + | [[Category: Condensing enzyme]] |
| - | [[Category: | + | [[Category: Fatty acid elongation]] |
| - | [[Category: | + | [[Category: Five-layered fold]] |
| - | [[Category: | + | [[Category: Lipid metabolism]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:30:56 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 19:30, 2 May 2008
BETA-KETOACYL-ACP SYNTHASE II FROM ESCHERICHIA COLI
Overview
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.
About this Structure
1KAS is a Single protein structure of sequence from Escherichia coli. The following page contains interesting information on the relation of 1KAS with [Fatty Acid Synthase]. Full crystallographic information is available from OCA.
Reference
Crystal structure of beta-ketoacyl-acyl carrier protein synthase II from E.coli reveals the molecular architecture of condensing enzymes., Huang W, Jia J, Edwards P, Dehesh K, Schneider G, Lindqvist Y, EMBO J. 1998 Mar 2;17(5):1183-91. PMID:9482715 Page seeded by OCA on Fri May 2 22:30:56 2008
Categories: Beta-ketoacyl-acyl-carrier-protein synthase I | Escherichia coli | Fatty Acid Synthase | Single protein | Dehesh, K. | Edwards, P. | Huang, W. | Jia, J. | Lindqvist, Y. | Schneider, G. | Acyltransferase | Alpha-beta protein | Alpha-beta-alpha-beta-alpha | Condensing enzyme | Fatty acid elongation | Five-layered fold | Lipid metabolism
