2CB9

Crystal structure of the thioesterase domain of the fengycin biosynthesis cluster

Summary for 2CB9

• Entry DOI: 10.2210/pdb2cb9/pdb
• Related: 2CBG
• Descriptor: FENGYCIN SYNTHETASE, ACETIC ACID (3 entities in total)
• Functional Keywords: thioesterase, non-ribosomal peptide synthesis, alpha/beta-hydrolases, catalytic triade, hydrolase
• Biological source: BACILLUS SUBTILIS
• Total number of polymer chains: 1
• Total formula weight: 27582.79

Authors

Samel, S.,Marahiel, M.A.,Essen, L.-O. (deposition date: 2006-01-03, release date: 2007-03-06, Last modification date: 2023-12-13)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.8 Å)