2cb9
From Proteopedia
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|PDB= 2cb9 |SIZE=350|CAPTION= <scene name='initialview01'>2cb9</scene>, resolution 1.80Å | |PDB= 2cb9 |SIZE=350|CAPTION= <scene name='initialview01'>2cb9</scene>, resolution 1.80Å | ||
|SITE= <scene name='pdbsite=AC1:Acy+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Acy+Binding+Site+For+Chain+A'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=ACY:ACETIC ACID'>ACY</scene> | + | |LIGAND= <scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2cb9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cb9 OCA], [http://www.ebi.ac.uk/pdbsum/2cb9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2cb9 RCSB]</span> | ||
}} | }} | ||
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[[Category: Marahiel, M A.]] | [[Category: Marahiel, M A.]] | ||
[[Category: Samel, S.]] | [[Category: Samel, S.]] | ||
| - | [[Category: ACY]] | ||
[[Category: alpha/beta-hydrolase]] | [[Category: alpha/beta-hydrolase]] | ||
[[Category: catalytic triade]] | [[Category: catalytic triade]] | ||
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[[Category: thioesterase]] | [[Category: thioesterase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:19:05 2008'' |
Revision as of 23:19, 30 March 2008
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| , resolution 1.80Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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