› 1o82

X-ray diffraction
1.46Å resolution

X-RAY STRUCTURE OF BACTERIOCIN AS-48 AT PH 4.5. SULPHATE BOUND FORM

Released:
DOI: 10.2210/pdb1o82/pdb
PDB entry 1o82 coloured by chain, front view.
PDB entry 1o82 coloured by chain, side view.
PDB entry 1o82 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 SO4 5 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: I222
Unit cell:
a: 79.473Å b: 83.405Å c: 99.828Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.208 0.223

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

Mechanisms of action of ribosomally synthesized and posttranslationally modified peptides (RiPPs).
Cao et al. (2021)
2 more