TITLE

Crystal structure of ß-ketoacyl-acyl carrier protein synthase II from E.coli reveals the molecular architecture of condensing enzymes

AUTHOR(S)
Weijun Huang; Jia, Jia; Edwards, Patricia; Dehesh, Katayoon; Schneider, Gunter; Lindqvist, Ylva
PUB. DATE
March 1998
SOURCE
EMBO Journal;3/1/98, Vol. 17 Issue 5, p1183
SOURCE TYPE
Academic Journal
DOC. TYPE
Article
ABSTRACT
In the biosynthesis of fatty acids, the β-ketoacylacyl 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 β-ketoacyl synthase II from Escherichia coli has been determined with the multiple isomorphous replacement method and refined at 2.4 Å resolution. The subunit consists of two mixed five-stranded β-sheets surrounded by α-helices. The two sheets are packed against each other in such a way that the fold can be described as consisting of five layers, α­β­α­β­α. 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 ∼25 Å 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 β-ketoacyl synthase is similar to that of thiolase, an enzyme involved in the β-oxidation pathway, indicating that both enzymes might have a common ancestor.
ACCESSION #
13006093

 

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