This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1kas

From Proteopedia

Revision as of 14:35, 5 November 2007 by OCA (Talk | contribs)
Jump to: navigation, search

1kas, resolution 2.4Å

Drag the structure with the mouse to rotate

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]. Active as Beta-ketoacyl-acyl-carrier-protein synthase I, with EC number 2.3.1.41 Structure known Active Site: ACT. 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 Mon Nov 5 16:41:07 2007

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools