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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Crystal structure of a cholera toxin-related heat-labile enterotoxin from E. coli.

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.[1]

References

  1. Crystal structure of a cholera toxin-related heat-labile enterotoxin from E. coli. Sixma, T.K., Pronk, S.E., Kalk, K.H., Wartna, E.S., van Zanten, B.A., Witholt, B., Hol, W.G. Nature (1991) [Pubmed]
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