2CBG

Crystal structure of the PMSF-inhibited thioesterase domain of the fengycin biosynthesis cluster

2CBG の概要

• エントリーDOI: 10.2210/pdb2cbg/pdb
• 関連するPDBエントリー: 2CB9
• 分子名称: FENGYCIN SYNTHETASE, phenylmethanesulfonic acid (3 entities in total)
• 機能のキーワード: fengycin thioesterase, non-ribosomal peptide synthesis, alpha/beta-hydrolase, phosphopantetheine, hydrolase
• 由来する生物種: BACILLUS SUBTILIS
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 27694.94

構造登録者

Samel, S.,Marahiel, M.A.,Essen, L.-O. (登録日: 2006-01-03, 公開日: 2007-03-06, 最終更新日: 2024-11-06)

主引用文献

Samel, S.,Wagner, B.,Marahiel, M.A.,Essen, L.-O.
The Thioesterase Domain of the Fengycin Biosynthesis Cluster: A Structural Base for the Macrocyclization of a Non-Ribosomal Lipopeptide
J.Mol.Biol., 359:876-, 2006

PubMed Abstract: 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.

PubMed: 16697411
DOI: 10.1016/J.JMB.2006.03.062

実験手法

X-RAY DIFFRACTION (2.5 Å)