1kas: Difference between revisions
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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'' | |||
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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
Proteopedia Page Contributors and Editors (what is this?)
- Pages with broken file links
- 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
