1hn9
From Proteopedia
|
CRYSTAL STRUCTURE OF BETA-KETOACYL-ACP SYNTHASE III
Overview
Beta-ketoacyl-acyl carrier protein synthase III (FabH), the most divergent, member of the family of condensing enzymes, is a key catalyst in bacterial, fatty acid biosynthesis and a promising target for novel antibiotics. We, report here the crystal structures of FabH determined in the presence and, absence of acetyl-CoA. These structures display a fold that is common for, condensing enzymes. The observed acetylation of Cys(112) proves its, catalytic role and clearly defines the primer binding pocket. Modeling, based on a bound CoA molecule suggests catalytic roles for His(244) and, Asn(274). The structures provide the molecular basis for FabH substrate, specificity and reaction mechanism and are important for structure-based, design of novel antibiotics.
About this Structure
1HN9 is a Single protein structure of sequence from Escherichia coli with PO4 as ligand. This structure superseeds the now removed PDB entry 1D9B. Active as Beta-ketoacyl-acyl-carrier-protein synthase I, with EC number 2.3.1.41 Full crystallographic information is available from OCA.
Reference
Crystal structure of beta-ketoacyl-acyl carrier protein synthase III. A key condensing enzyme in bacterial fatty acid biosynthesis., Qiu X, Janson CA, Konstantinidis AK, Nwagwu S, Silverman C, Smith WW, Khandekar S, Lonsdale J, Abdel-Meguid SS, J Biol Chem. 1999 Dec 17;274(51):36465-71. PMID:10593943
Page seeded by OCA on Tue Nov 20 16:40:10 2007
