Published August 1, 1995
| Version v1
Journal article
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The three-dimensional crystal structure of cholera toxin
Creators
- Westbrook, Mary L.
- Zhang, Rong-Guang; Westbrook M L.; Nance S.; Spangler B D. Argonne National Lab. IL (United States)
- Scott, David L. Yale Univ New Haven CT (United States). Dept of Molecular Biophysics and Biochemistry
- Nance, Sharon
- Spangler, Brenda D.
- Shipley, Graham G.
- Westbrook, Edwin M. Northwestern Univ Evanston IL (United States)
Description
The clinical manifestations of cholera are largely attributable to the actions of a secreted hexameric AB{sub 5} enterotoxin (choleragen). We have solved the three-dimensional structure of choleragen at 2.5 {Angstrom} resolution and compared the refined coordinates with those of choleragenoid (isolated B pentamer) and the heat-labile enterotoxin from Escherichia coli (LT). The crystalline coordinates provide a detailed view of the stereochemistry implicated in binding to GM1 gangliosides and in carrying out ADP-ribosylation. The A2 chain of choleragen, in contrast to that of LT, is a nearly continuous {alpha}-helix with an interpretable carboxyl tail.
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