DOI: 10.1073/pnas.83.5.1320. Structure of exotoxin A of Pseudomonas aeruginosa at 3.0-Angstrom resolution.

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

10.1073/pnas.83.5.1320

Crossref journal-article

Proceedings of the National Academy of Sciences

Proceedings of the National Academy of Sciences (341)

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.

Bibliography

Allured, V. S., Collier, R. J., Carroll, S. F., & McKay, D. B. (1986). Structure of exotoxin A of Pseudomonas aeruginosa at 3.0-Angstrom resolution. Proceedings of the National Academy of Sciences, 83(5), 1320â1324.

Authors 4

V S Allured (first)
R J Collier (additional)
S F Carroll (additional)
D B McKay (additional)

References 0 Referenced 372

None

Dates

Type	When
Created	19 years, 3 months ago (May 31, 2006, 6:13 a.m.)
Deposited	3 years, 4 months ago (April 13, 2022, 12:22 p.m.)
Indexed	1 month ago (Aug. 2, 2025, 12:08 a.m.)
Issued	39 years, 6 months ago (March 1, 1986)
Published	39 years, 6 months ago (March 1, 1986)
Published Online	39 years, 6 months ago (March 1, 1986)
Published Print	39 years, 6 months ago (March 1, 1986)

Funders 0

None

BibTeX

@article{Allured_1986, title={Structure of exotoxin A of Pseudomonas aeruginosa at 3.0-Angstrom resolution.}, volume={83}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.83.5.1320}, DOI={10.1073/pnas.83.5.1320}, number={5}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Allured, V S and Collier, R J and Carroll, S F and McKay, D B}, year={1986}, month=mar, pages={1320–1324} }

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