1kas
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BETA-KETOACYL-ACP SYNTHASE II FROM ESCHERICHIA COLI
OverviewOverview
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 ... [(full description)]
About this StructureAbout 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]. Active as [Transferase], with EC number [2.3.1.41]. Structure known Active Site: ACT. Full crystallographic information is available from [OCA].
ReferenceReference
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
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