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1dd8
From Proteopedia
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CRYSTAL STRUCTURE OF BETA-KETOACYL-[ACYL CARRIER PROTEIN] SYNTHASE I FROM ESCHERICHIA COLI
Overview
The crystal structure of the fatty acid elongating enzyme beta-ketoacyl, [acyl carrier protein] synthase I (KAS I) from Escherichia coli has been, determined to 2.3 A resolution by molecular replacement using the recently, solved crystal structure of KAS II as a search model. The crystal contains, two independent dimers in the asymmetric unit. KAS I assumes the thiolase, alpha(beta)alpha(beta)alpha fold. Electrostatic potential distribution, reveals an acyl carrier protein docking site and a presumed substrate, binding pocket was detected extending the active site. Both subunits, contribute to each substrate binding site in the dimer.
About this Structure
1DD8 is a Single protein structure of sequence from Escherichia coli. Active as Beta-ketoacyl-acyl-carrier-protein synthase I, with EC number 2.3.1.41 Full crystallographic information is available from OCA.
Reference
The X-ray crystal structure of beta-ketoacyl [acyl carrier protein] synthase I., Olsen JG, Kadziola A, von Wettstein-Knowles P, Siggaard-Andersen M, Lindquist Y, Larsen S, FEBS Lett. 1999 Oct 22;460(1):46-52. PMID:10571059
Page seeded by OCA on Tue Nov 20 13:11:22 2007
