› 1xk9

X-ray diffraction
2.1Å resolution

Pseudomanas exotoxin A in complex with the PJ34 inhibitor

Released:
DOI: 10.2210/pdb1xk9/pdb
PDB entry 1xk9 coloured by chain, front view.
PDB entry 1xk9 coloured by chain, side view.
PDB entry 1xk9 coloured by chain, top view.
Source organism: Pseudomonas aeruginosa
Primary publication:
Structure-function analysis of water-soluble inhibitors of the catalytic domain of exotoxin A from Pseudomonas aeruginosa.
Yates SP, Taylor PL, Jørgensen R, Ferraris D, Zhang J, Andersen GR, Merrill AR
Biochem J 385 667-75 (2005)
PMID: 15458385

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145826 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Exotoxin A Chains: A, B
Molecule details ›
Chains: A, B
Length: 215 amino acids
Theoretical weight: 23.46 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli
UniProt:
  • Canonical: P11439 (Residues: 424-638; Coverage: 35%)
Gene names: PA1148, eta
Sequence domains: Exotoxin A catalytic
Structure domains: Diphtheria Toxin, domain 1

Ligands and Environments

1 bound ligand:
Ligand P34 2 x P34
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I911-2
Spacegroup: P212121
Unit cell:
a: 56.04Å b: 78.68Å c: 91.69Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.214 0.213 0.235
Expression system: Escherichia coli

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Citations

5 review citations

Nuclear ADP-ribosylation reactions in mammalian cells: where are we today and where are we going?
Hassa et al. (2006)
4 more

12 mentions without citation

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