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. 1986 Mar;83(5):1320-4.
doi: 10.1073/pnas.83.5.1320.

Structure of exotoxin A of Pseudomonas aeruginosa at 3.0-Angstrom resolution

V S Allured, R J Collier, S F Carroll, D B McKay

Structure of exotoxin A of Pseudomonas aeruginosa at 3.0-Angstrom resolution

V S Allured et al. Proc Natl Acad Sci U S A. 1986 Mar.

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.

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