1l0i

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Revision as of 06:56, 18 November 2007

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spinqualitylabelsall models 1l0i, resolution 1.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of butyryl-ACP I62M mutant

Overview

Acyl carrier protein (ACP) is an essential cofactor in biosynthesis of, fatty acids and many other reactions that require acyl transfer steps. We, have determined the first crystal structures of an acylated form of ACP, from E. coli, that of butyryl-ACP. Our analysis of the molecular surface, of ACP reveals a plastic hydrophobic cavity in the vicinity of the, phosphopantethylated Ser36 residue that is expanded and occupied by the, butyryl and beta-mercaptoethylamine moieties of the acylated, 4'-phosphopantetheine group in one of our crystal forms. In the other, form, the cavity is contracted, and we propose that the protein has, adopted the conformation after delivery of substrate into the active site, of a partner enzyme.

About this Structure

1L0I is a Single protein structure of sequence from Escherichia coli with NA, ZN, CAC and PSR as ligands. The following page contains interesting information on the relation of 1L0I with [Fatty Acid Synthase]. Full crystallographic information is available from OCA.

Reference

X-ray crystallographic studies on butyryl-ACP reveal flexibility of the structure around a putative acyl chain binding site., Roujeinikova A, Baldock C, Simon WJ, Gilroy J, Baker PJ, Stuitje AR, Rice DW, Slabas AR, Rafferty JB, Structure. 2002 Jun;10(6):825-35. PMID:12057197

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