› 4ozk

X-ray diffraction
2.04Å resolution

Crystal structure of Laterosporulin, a broad spectrum leaderless bacteriocin produced by Brevibacillus laterosporus strain GI-9

Released:
DOI: 10.2210/pdb4ozk/pdb
PDB entry 4ozk coloured by chain, front view.
PDB entry 4ozk coloured by chain, side view.
PDB entry 4ozk coloured by chain, top view.
Source organism: Brevibacillus laterosporus GI-9
Primary publication:
The intramolecular disulfide-stapled structure of laterosporulin, a class IId bacteriocin, conceals a human defensin-like structural module.
Singh PK, Solanki V, Sharma S, Thakur KG, Krishnan B, Korpole S
FEBS J 282 203-14 (2015)
PMID: 25345978

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-124726 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Putative bacteriocin Chain: A
Molecule details ›
Chain: A
Length: 49 amino acids
Theoretical weight: 5.63 KDa
Source organism: Brevibacillus laterosporus GI-9
UniProt:
  • Canonical: H1ZZ98 (Residues: 2-50; Coverage: 98%)
Gene name: laterosporulin
Sequence domains: Laterosporulin defensin-like peptide

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P4332
Unit cell:
a: 65Å b: 65Å c: 65Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.196 0.227

Quick links

Citations

10 review citations

The expanding structural variety among bacteriocins from Gram-positive bacteria.
Acedo et al. (2018)
9 more

1 mention without citation

Stapled Peptides Inhibitors: A New Window for Target Drug Discovery.
Ali et al. (2019)