› 1y2v

X-ray diffraction
1.9Å resolution

Crystal structure of the common edible mushroom (Agaricus bisporus) lectin in complex with T-antigen

Released:
DOI: 10.2210/pdb1y2v/pdb
PDB entry 1y2v coloured by chain, front view.
PDB entry 1y2v coloured by chain, side view.
PDB entry 1y2v coloured by chain, top view.
Source organism: Agaricus bisporus
Primary publication:
The antineoplastic lectin of the common edible mushroom (Agaricus bisporus) has two binding sites, each specific for a different configuration at a single epimeric hydroxyl.
Carrizo ME, Capaldi S, Perduca M, Irazoqui FJ, Nores GA, Monaco HL
J Biol Chem 280 10614-23 (2005)
PMID: 15596442

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-169390 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Agaricus bisporus lectin Chains: A, B
Molecule details ›
Chains: A, B
Length: 142 amino acids
Theoretical weight: 16.07 KDa
Source organism: Agaricus bisporus
UniProt:
  • Canonical: Q00022 (Residues: 2-143; Coverage: 99%)
Sequence domains: Fungal fruit body lectin
Structure domains: Cytolysin/lectin

Ligands and Environments

Carbohydrate polymer : NEW Components: NGA, GAL
Carbohydrate polymer
1 bound ligand:
Ligand SER 2 x SER
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: C2221
Unit cell:
a: 91.86Å b: 96.16Å c: 75.08Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.195 0.212

Quick links

Citations

12 review citations

Disparate proteins use similar architectures to damage membranes.
Anderluh et al. (2008)
11 more

2 mentions without citation

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