› 1w3a

X-ray diffraction
2.65Å resolution

Three dimensional structure of a novel pore-forming lectin from the mushroom Laetiporus sulphureus

Released:
DOI: 10.2210/pdb1w3a/pdb
PDB entry 1w3a coloured by chain, front view.
PDB entry 1w3a coloured by chain, side view.
PDB entry 1w3a 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: GLC, GAL
Carbohydrate polymer
1 bound ligand:
Ligand GOL 6 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P6322
Unit cell:
a: 101.526Å b: 101.526Å c: 193.435Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.229 0.226 0.28

Quick links

Citations

16 review citations

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

10 mentions without citation

Structural insights into Bacillus thuringiensis Cry, Cyt and parasporin toxins.
Xu et al. (2014)
9 more