Mapping the enzymatic active site of Pseudomonas aeruginosa exotoxin A
Copyright policy )Mapping the enzymatic active site of Pseudomonas aeruginosa exotoxin A
AbstractPseudomonas aeruginosa exotoxin A is representative of a class of enzymes, the monoADP‐ribosyl, which catalyze the covalent transfer of an ADP‐ribose moiety of NAD+ to a target substrate. Availability of the three‐dimensional structure of exotoxin A provides the opportunity for mapping substrate binding sites and suggesting which amino acid residues may be involved in catalysis. Data from several sources have been combined to develop a proposal for the NAD+ binding site of exotoxin A: the binding of NAD+ fragments adenosine, AMP, and ADP have been delineated crystallographically to 6.0, 6.0, and 2.7 Å, respectively; significant sequence homology spanning 60 residues has been found between exotoxin A and diphtheria toxin, which has the identical enzymatic activity; iodination of exotoxin A, under conditions in which only tyrosine 481 is iodinated in the enzymatic domain, abolishes ADP‐ribosyl transferase activity.
- University of Colorado System United States
- University of Colorado Boulder United States
ADP Ribose Transferases, Models, Molecular, Binding Sites, Crystallography, Fourier Analysis, Virulence Factors, Bacterial Toxins, Molecular Sequence Data, Exotoxins, Ligands, NAD, Peptide Mapping, Pseudomonas aeruginosa, Tetranitromethane, Diphtheria Toxin, Amino Acid Sequence, Pseudomonas aeruginosa Exotoxin A, Iodine
ADP Ribose Transferases, Models, Molecular, Binding Sites, Crystallography, Fourier Analysis, Virulence Factors, Bacterial Toxins, Molecular Sequence Data, Exotoxins, Ligands, NAD, Peptide Mapping, Pseudomonas aeruginosa, Tetranitromethane, Diphtheria Toxin, Amino Acid Sequence, Pseudomonas aeruginosa Exotoxin A, Iodine
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