› 1nli

X-ray diffraction
1.93Å resolution

Complex of [E160A-E189A] trichosanthin and adenine

Released:
DOI: 10.2210/pdb1nli/pdb
PDB entry 1nli coloured by chain, front view.
PDB entry 1nli coloured by chain, side view.
PDB entry 1nli coloured by chain, top view.
Source organism: Trichosanthes kirilowii
Primary publication:
Structural basis for the interaction of [E160A-E189A]-trichosanthin with adenine.
Shaw PC, Wong KB, Chan DS, Williams RL
Toxicon 41 575-81 (2003)
PMID: 12676436

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-140879 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribosome-inactivating protein alpha-trichosanthin Chain: A
Molecule details ›
Chain: A
Length: 248 amino acids
Theoretical weight: 27.18 KDa
Source organism: Trichosanthes kirilowii
Expression system: Escherichia coli
UniProt:
  • Canonical: P09989 (Residues: 24-270; Coverage: 93%)
Sequence domains: Ribosome inactivating protein
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand ADE 1 x ADE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P212121
Unit cell:
a: 37.928Å b: 75.299Å c: 78.65Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.16 0.158 0.208
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Recent advances in trichosanthin, a ribosome-inactivating protein with multiple pharmacological properties.
Shaw et al. (2005)
4 other articles

1 mention without citation

Substrate specificity of bacterial endoribonuclease toxins.
Han et al. (2020)