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Nature. 1991 May 30;351(6325):371-7.

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

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1
BIOSON Research Institute, Groningen, The Netherlands.

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.

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PMID:
2034287
DOI:
10.1038/351371a0
[Indexed for MEDLINE]

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