› 2oqa

X-ray diffraction
1.4Å resolution

X-ray Sequence and Crystal Structure of Luffaculin 1, a Novel Type 1 Ribosome-inactivating Protein

Released:
DOI: 10.2210/pdb2oqa/pdb
PDB entry 2oqa coloured by chain, front view.
PDB entry 2oqa coloured by chain, side view.
PDB entry 2oqa coloured by chain, top view.
Source organism: Luffa acutangula
Primary publication:
X-ray sequence and crystal structure of luffaculin 1, a novel type 1 ribosome-inactivating protein.
Hou X, Chen M, Chen L, Meehan EJ, Xie J, Huang M
BMC Struct Biol 7 29 (2007)
PMID: 17470286

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 analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160892 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribosome-inactivating protein luffaculin 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 241 amino acids
Theoretical weight: 25.91 KDa
Source organism: Luffa acutangula
UniProt:
  • Canonical: P84530 (Residues: 1-241; Coverage: 100%)
Sequence domains: Ribosome inactivating protein
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand NAG 4 x NAG
Ligand PG4 1 x PG4
Ligand PEG 2 x PEG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P1
Unit cell:
a: 39.135Å b: 46.813Å c: 83.571Å
α: 89.07° β: 80.01° γ: 72.14°
R-values:
R R work R free
0.214 0.213 0.232

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)
6 other articles

3 mentions without citation

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