2cb9
From Proteopedia
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==Overview== | ==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 . | + | 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== | ==About this Structure== | ||
| - | 2CB9 is a | + | 2CB9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with ACY as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CB9 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: thioesterase]] | [[Category: thioesterase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 15:08:06 2007'' |
Revision as of 13:02, 5 November 2007
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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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