1jmk
From Proteopedia
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Structural Basis for the Cyclization of the Lipopeptide Antibiotic Surfactin by the Thioesterase Domain SrfTE
Overview
Many biologically active natural peptides are synthesized by nonribosomal, peptide synthetases (NRPS). Product release is accomplished by dedicated, thioesterase (TE) domains, some of which catalyze an intramolecular, cyclization to form macrolactone or macrolactam cyclic peptides. The, excised 28 kDa SrfTE domain, a member of the alpha/beta hydrolase enzyme, family, exhibits a distinctive bowl-shaped hydrophobic cavity that hosts, the acylpeptide substrate and tolerates its folding to form a cyclic, structure. A substrate analog confirms the substrate binding site and, suggests a mechanism for substrate acylation/deacylation. Docking of the, peptidyl carrier protein domain immediately preceding SrfTE positions the, 4'-phosphopantheinyl prosthetic group that transfers the nascent, acyl-peptide chain to SrfTE. The structure provides a basis for, understanding the mechanism of acyl-PCP substrate recognition and for the, cyclization reaction that results in release of the macrolactone cyclic, heptapeptide.
About this Structure
1JMK is a Single protein structure of sequence from Bacillus subtilis with SO4 as ligand. Full crystallographic information is available from OCA.
Reference
Structural basis for the cyclization of the lipopeptide antibiotic surfactin by the thioesterase domain SrfTE., Bruner SD, Weber T, Kohli RM, Schwarzer D, Marahiel MA, Walsh CT, Stubbs MT, Structure. 2002 Mar;10(3):301-10. PMID:12005429
Page seeded by OCA on Tue Nov 20 18:22:46 2007
