› 1w3f

X-ray diffraction
2.58Å resolution

Crystal structure of the hemolytic lectin from the mushroom Laetiporus sulphureus complexed with N-acetyllactosamine in the gamma motif

Released:
DOI: 10.2210/pdb1w3f/pdb
PDB entry 1w3f coloured by chain, front view.
PDB entry 1w3f coloured by chain, side view.
PDB entry 1w3f coloured by chain, top view.
Source organism: Laetiporus sulphureus
Primary publication:
Structural analysis of the Laetiporus sulphureus hemolytic pore-forming lectin in complex with sugars.
Mancheño JM, Tateno H, Goldstein IJ, Martínez-Ripoll M, Hermoso JA
J Biol Chem 280 17251-9 (2005)
PMID: 15687495

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-182315 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Hemolytic lectin LSLa Chain: A
Molecule details ›
Chain: A
Length: 315 amino acids
Theoretical weight: 35.12 KDa
Source organism: Laetiporus sulphureus
UniProt:
  • Canonical: Q7Z8V1 (Residues: 1-315; Coverage: 100%)
Gene name: lsla
Sequence domains: Clostridium epsilon toxin ETX/Bacillus mosquitocidal toxin MTX2
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NDG, GAL
Carbohydrate polymer
1 bound ligand:
Ligand GOL 5 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF NONIUS
Spacegroup: P6322
Unit cell:
a: 101.76Å b: 101.76Å c: 193.03Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.231 0.231 0.272

Quick links

Citations

17 review citations

Pore-forming toxins: ancient, but never really out of fashion.
Dal Peraro et al. (2016)
16 more

5 mentions without citation

Mushroom lectins: specificity, structure and bioactivity relevant to human disease.
Hassan et al. (2015)
4 more