Crystal structure of a cholera toxin-related heat-labile enterotoxin from E. coli.
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Sixma TK, Pronk SE, Kalk KH, Wartna ES, van Zanten BA, Witholt B, Hol WG
Crystal structure of a cholera toxin-related heat-labile enterotoxin from E. coli.
Nature. 1991 May 30;351(6325):371-7.
- PubMed ID
- 2034287 [ View in PubMed]
- 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.