› 2cb9

X-ray diffraction
1.8Å resolution

Crystal structure of the thioesterase domain of the fengycin biosynthesis cluster

Released:
DOI: 10.2210/pdb2cb9/pdb
PDB entry 2cb9 coloured by chain, front view.
PDB entry 2cb9 coloured by chain, side view.
PDB entry 2cb9 coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
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 359 876-89 (2006)
PMID: 16697411

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-175058 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carrier domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 244 amino acids
Theoretical weight: 27.52 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q45563 (Residues: 1039-1274; Coverage: 19%)
Gene name: fenB
Sequence domains: Thioesterase domain
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand ACY 1 x ACY
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR591
Spacegroup: P61
Unit cell:
a: 72.354Å b: 72.354Å c: 96.333Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.152 0.15 0.188
Expression system: Escherichia coli

Quick links

Citations

25 review citations

Natural functions of lipopeptides from Bacillus and Pseudomonas: more than surfactants and antibiotics.
Raaijmakers et al. (2010)
24 more

6 mentions without citation

Thioesterases: a new perspective based on their primary and tertiary structures.
Cantu et al. (2010)
5 more