Crystal structure of a cholera toxin-related heat-labile enterotoxin from E. coli
- 1 May 1991
- journal article
- Published by Springer Nature in Nature
- Vol. 351 (6325) , 371-377
- https://doi.org/10.1038/351371a0
Abstract
Examination of the structure of Escherichia coli heat-labile enterotoxin in the AB5 complex at a resolution of 2.3A reveals that the doughnut-shaped B pentamer binds the enzymatic A subunit using a hairpin of the A2 fragment, through a highly charged central pore. Putative ganglioside GM1-binding sites on the B subunits are more than 20A removed from the membrane-crossing A1 subunit. This ADP-ribosylating (A1) fragment of the toxin has structural homology with the catalytic region of exotoxin A and hence also to diphtheria toxin.Keywords
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