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1hnd
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(New page: 200px<br /><applet load="1hnd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hnd, resolution 1.6Å" /> '''CRYSTAL STRUCTURE OF ...)
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Revision as of 14:33, 20 November 2007
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CRYSTAL STRUCTURE OF BETA-KETOACYL-ACP SYNTHASE III-COA COMPLEX
Overview
beta-Ketoacyl-acyl carrier protein synthase III (FabH) is a condensing, enzyme that plays central roles in fatty acid biosynthesis., Three-dimensional structures of E. coli FabH in the presence and absence, of ligands have been refined to 1.46 A resolution. The structures of, improved accuracy revealed detailed interactions involved in ligand, binding. These structures also provided new insights into the FabH, mechanism, e.g. the possible role of a water or hydroxyl anion in Cys112, deprotonation. A structure of the apo enzyme uncovered large, conformational changes in the active site, exemplified by the disordering, of four essential loops (84-86, 146-152, 185-217 and 305-307) and the, movement of catalytic residues (Cys112 and His244). The disordering of the, loops leads to greater than 50 % reduction in the FabH dimer interface, suggesting a dynamic nature for an unusually large portion of the dimer, interface. The existence of a large solvent-accessible channel in the, dimer interface as well as two cis-peptides (cis-Pro88 and cis-Phe308) in, two of the disordered loops may explain the observed structural, instabilities.
About this Structure
1HND is a Single protein structure of sequence from Escherichia coli with COA as ligand. Active as Beta-ketoacyl-acyl-carrier-protein synthase I, with EC number 2.3.1.41 Full crystallographic information is available from OCA.
Reference
Refined structures of beta-ketoacyl-acyl carrier protein synthase III., Qiu X, Janson CA, Smith WW, Head M, Lonsdale J, Konstantinidis AK, J Mol Biol. 2001 Mar 16;307(1):341-56. PMID:11243824
Page seeded by OCA on Tue Nov 20 16:40:16 2007
