› 1aer

X-ray diffraction
2.3Å resolution

DOMAIN III OF PSEUDOMONAS AERUGINOSA EXOTOXIN COMPLEXED WITH BETA-TAD

Released:
DOI: 10.2210/pdb1aer/pdb
PDB entry 1aer coloured by chain, front view.
PDB entry 1aer coloured by chain, side view.
PDB entry 1aer coloured by chain, top view.
Source organism: Pseudomonas aeruginosa
Primary publication:
Crystal structure of the catalytic domain of Pseudomonas exotoxin A complexed with a nicotinamide adenine dinucleotide analog: implications for the activation process and for ADP ribosylation.
Li M, Dyda F, Benhar I, Pastan I, Davies DR
Proc Natl Acad Sci U S A 93 6902-6 (1996)
PMID: 8692916

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:
  • not assigned
Sequence domain:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145828 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Exotoxin A Chains: A, B
Molecule details ›
Chains: A, B
Length: 211 amino acids
Theoretical weight: 22.92 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli
UniProt:
  • Canonical: P11439 (Residues: 425-634; Coverage: 34%)
Gene names: PA1148, eta
Sequence domains: Exotoxin A catalytic
Structure domains: Diphtheria Toxin, domain 1

Ligands and Environments


Cofactor: Ligand TAD 1 x TAD
2 bound ligands:
Ligand TIA 1 x TIA
Ligand AMP 1 x AMP
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P43212
Unit cell:
a: 87.64Å b: 87.64Å c: 133.73Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.196 0.285
Expression system: Escherichia coli

Quick links

Citations

19 review citations

Binary bacterial toxins: biochemistry, biology, and applications of common Clostridium and Bacillus proteins.
Barth et al. (2004)
18 more

7 mentions without citation

Development of Anti-Virulence Therapeutics against Mono-ADP-Ribosyltransferase Toxins.
Lugo et al. (2020)
6 more