The three-dimensional crystal structure of cholera toxin
- Argonne National Lab., IL (United States)
- Yale Univ., New Haven, CT (United States). Dept. of Molecular Biophysics and Biochemistry
- Northwestern Univ., Evanston, IL (United States)
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.
- Research Organization:
- Argonne National Lab., IL (United States)
- Sponsoring Organization:
- USDOE, Washington, DC (United States)
- DOE Contract Number:
- W-31109-ENG-38
- OSTI ID:
- 205782
- Report Number(s):
- ANL/CMB/PP--83551; ON: DE96006540
- Country of Publication:
- United States
- Language:
- English
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