title: Structure of exotoxin A of Pseudomonas aeruginosa at 3.0-Angstrom resolution.
abstract: Exotoxin A of Pseudomonas aeruginosa is a secreted bacterial toxin capable of translocating a catalytic domain into mammalian cells and inhibiting protein synthesis by the ADP-ribosylation of cellular elongation factor 2. The protein is a single polypeptide chain of 613 amino acids. The x-ray crystallographic structure of exotoxin A, determined to 3.0-A resolution, shows the following: an amino-terminal domain, composed primarily of antiparallel beta-structure and comprising approximately half of the molecule; a middle domain composed of alpha-helices; and a carboxyl-terminal domain comprising approximately one-third of the molecule. The carboxyl-terminal domain is the ADP-ribosyltransferase of the toxin. The other two domains are presumably involved in cell receptor binding and membrane translocation.
mesh_terms: D036002:ADP Ribose Transferases; D001427:Bacterial Toxins; D001692:Biological Transport; D002352:Carrier Proteins; D004792:Enzyme Precursors; D005098:Exotoxins; D008958:Models, Molecular; D009713:Nucleotidyltransferases; D011065:Poly(ADP-ribose) Polymerases; D011487:Protein Conformation; D011550:Pseudomonas aeruginosa; D011956:Receptors, Cell Surface; D011950:Receptors, Cholinergic / Q000378:metabolism; D012995:Solubility; D037521:Virulence Factors; D014961:X-Ray Diffraction; D000097668:Pseudomonas aeruginosa Exotoxin A
chemical_list: D036002:ADP Ribose Transferases; D001427:Bacterial Toxins; D002352:Carrier Proteins; D004792:Enzyme Precursors; D005098:Exotoxins; D009713:Nucleotidyltransferases; D011065:Poly(ADP-ribose) Polymerases; D011956:Receptors, Cell Surface; D011950:Receptors, Cholinergic; D037521:Virulence Factors; D000097668:Pseudomonas aeruginosa Exotoxin A; C027553:Pseudomonas exotoxin binding protein, mouse