Abstract
Examination of the structure of Escherichia coli heat-labile enterotoxin in the AB5 complex at a resolution of 2.3 Å 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 20 Å removed from the membrane-crossing Al subunit. This ADP-ribosylating (Al) fragment of the toxin has structural homology with the catalytic region of exotoxin A and hence also to diphtheria toxin.
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Sixma, T., Pronk, S., Kalk, K. et al. Crystal structure of a cholera toxin-related heat-labile enterotoxin from E. coli. Nature 351, 371–377 (1991). https://doi.org/10.1038/351371a0
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DOI: https://doi.org/10.1038/351371a0
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