2cb9: Difference between revisions

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[[Image:2cb9.gif|left|200px]]
{{Seed}}
[[Image:2cb9.png|left|200px]]


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{{STRUCTURE_2cb9|  PDB=2cb9  |  SCENE=  }}  
{{STRUCTURE_2cb9|  PDB=2cb9  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF THE THIOESTERASE DOMAIN OF THE FENGYCIN BIOSYNTHESIS CLUSTER'''
===CRYSTAL STRUCTURE OF THE THIOESTERASE DOMAIN OF THE FENGYCIN BIOSYNTHESIS CLUSTER===




==Overview==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_16697411}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 16697411 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16697411}}


==About this Structure==
==About this Structure==
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[[Category: Non-ribosomal peptide synthesis]]
[[Category: Non-ribosomal peptide synthesis]]
[[Category: Thioesterase]]
[[Category: Thioesterase]]
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