› 1dtp

X-ray diffraction
2.5Å resolution

THE STRUCTURE OF THE ISOLATED CATALYTIC DOMAIN OF DIPHTHERIA TOXIN

Released:
DOI: 10.2210/pdb1dtp/pdb
PDB entry 1dtp coloured by chain, front view.
PDB entry 1dtp coloured by chain, side view.
PDB entry 1dtp coloured by chain, top view.
Source organism: Corynephage beta
Primary publication:
Structure of the isolated catalytic domain of diphtheria toxin.
Weiss MS, Blanke SR, Collier RJ, Eisenberg D
Biochemistry 34 773-81 (1995)
PMID: 7827036

Function and Biology Details

Reaction catalysed: 
NAD(+) + diphthamide-[translation elongation factor 2] = nicotinamide + N-(ADP-D-ribosyl)diphthamide-[translation elongation factor 2]
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132742 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Diphtheria toxin fragment A Chain: A
Molecule details ›
Chain: A
Length: 190 amino acids
Theoretical weight: 20.77 KDa
Source organism: Corynephage beta
Expression system: Not provided
UniProt:
  • Canonical: P00588 (Residues: 33-222; Coverage: 36%)
Sequence domains: Diphtheria toxin, C domain
Structure domains: Diphtheria Toxin, domain 1

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2
Unit cell:
a: 55.7Å b: 43.9Å c: 73.9Å
α: 90° β: 101.5° γ: 90°
R-values:
R R work R free
0.197 0.197 not available
Expression system: Not provided

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Citations

3 review citations

Pore-forming protein toxins: from structure to function.
Parker et al. (2005)
2 more

5 mentions without citation

ADP-ribosylation systems in bacteria and viruses.
Mikolčević et al. (2021)
4 more