2cb9

From Proteopedia

Revision as of 15:59, 5 November 2007

CRYSTAL STRUCTURE OF THE THIOESTERASE DOMAIN OF THE FENGYCIN BIOSYNTHESIS CLUSTER

Overview

Many secondary metabolic peptides from bacteria and fungi are produced by, non-ribosomal peptide synthetases (NRPS) where the final step of, biosynthesis is often catalysed by designated thioesterase domains. Here, we report the 1.8A crystal structure of the fengycin thioesterase (FenTE), from Bacillus subtilis F29-3, which catalyses the regio- and, stereoselective release and macrocyclization of the antibiotic fengycin, from the NRPS template. A structure of the PMSF-inactivated FenTE domain, suggests the location of the oxyanion hole and the binding site of the, C-terminal residue l-Ile11 of the lipopeptide. Using a combination of, docking, molecular dynamics simulations and in vitro activity assays, a, model of the FenTE-fengycin complex was derived in which peptide, cyclization requires strategic interactions with residues lining the, active site canyon.

About this Structure

2CB9 is a Single protein structure of sequence from Bacillus subtilis with ACY as ligand. Structure known Active Site: AC1. Full crystallographic information is available from OCA.

Reference

The thioesterase domain of the fengycin biosynthesis cluster: a structural base for the macrocyclization of a non-ribosomal lipopeptide., Samel SA, Wagner B, Marahiel MA, Essen LO, J Mol Biol. 2006 Jun 16;359(4):876-89. Epub 2006 Apr 18. PMID:16697411

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