› 1o83

X-ray diffraction
1.64Å resolution

Crystal Structure of Bacteriocin AS-48 at pH 7.5, phosphate bound. Crystal form I

Released:
DOI: 10.2210/pdb1o83/pdb
PDB entry 1o83 coloured by chain, front view.
PDB entry 1o83 coloured by chain, side view.
PDB entry 1o83 coloured by chain, top view.
Source organism: Enterococcus faecalis
Primary publication:
Structure of bacteriocin AS-48: from soluble state to membrane bound state.
Sánchez-Barrena MJ, Martínez-Ripoll M, Gálvez A, Valdivia E, Maqueda M, Cruz V, Albert A
J Mol Biol 334 541-9 (2003)
PMID: 14623193

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-175269 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
BacA Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 70 amino acids
Theoretical weight: 7.18 KDa
Source organism: Enterococcus faecalis
UniProt:
  • Canonical: Q47765 (Residues: 36-105; Coverage: 67%)
Gene names: as-48, as48A, bacA
Sequence domains: Bacteriocin class IId cyclical uberolysin-like
Structure domains: Bacteriocin AS-48

Ligands and Environments

2 bound ligands:
Ligand GOL 1 x GOL
Ligand PO4 2 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: I222
Unit cell:
a: 79.67Å b: 83.88Å c: 99.77Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.193 0.215

Quick links

Citations

18 review citations

Ribosomally synthesized and post-translationally modified peptide natural products: overview and recommendations for a universal nomenclature.
Arnison et al. (2013)
17 more

3 mentions without citation

Antibacterial activities of bacteriocins: application in foods and pharmaceuticals.
Yang et al. (2014)
2 more