› 1nio

X-ray diffraction
2Å resolution

Crystal structure of beta-luffin, a ribosome inactivating protein at 2.0A resolution

Released:
DOI: 10.2210/pdb1nio/pdb
PDB entry 1nio coloured by chain, front view.
PDB entry 1nio coloured by chain, side view.
PDB entry 1nio coloured by chain, top view.
Source organism: Luffa aegyptiaca
Primary publication:
Crystal structure of beta-luffin, a ribosome-inactivating protein, at 2.0 A resolution.
Ma QJ, Li JH, Li HG, Wu S, Dong YC
Acta Crystallogr D Biol Crystallogr 59 1366-70 (2003)
PMID: 12876337

Function and Biology Details

Reaction catalysed: 
Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149812 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribosome-inactivating protein luffin-B Chain: A
Molecule details ›
Chain: A
Length: 247 amino acids
Theoretical weight: 27.1 KDa
Source organism: Luffa aegyptiaca
Expression system: Escherichia coli
UniProt:
  • Canonical: P22851 (Residues: 1-250; Coverage: 99%)
Sequence domains: Ribosome inactivating protein
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand NAG 3 x NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: C2
Unit cell:
a: 89.902Å b: 59.823Å c: 55.184Å
α: 90° β: 120.81° γ: 90°
R-values:
R R work R free
0.162 0.162 0.203
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Biological activities of ribosome-inactivating proteins and their possible applications as antimicrobial, anticancer, and anti-pest agents and in neuroscience research.
Akkouh et al. (2015)
3 other articles

5 mentions without citation

Structures and Ribosomal Interaction of Ribosome-Inactivating Proteins.
Shi et al. (2016)
4 more