1dd8

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(New page: 200px<br /><applet load="1dd8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dd8, resolution 2.3&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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Revision as of 11:04, 20 November 2007

Image:1dd8.gif

1dd8, resolution 2.3Å

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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

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