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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| rdf:type | |
| rdfs:comment |
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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| skos:exactMatch | |
| uniprot:name |
Nature
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| uniprot:author |
Hol W.G.J.,
Kalk K.H.,
Pronk S.E.,
Sixma T.K.,
Wartna E.S.,
Witholt B.,
van Zanten B.A.M.
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| uniprot:date |
1991
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| uniprot:pages |
371-377
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| uniprot:title |
Crystal structure of a cholera toxin-related heat-labile enterotoxin from E. coli.
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| uniprot:volume |
351
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| dc-term:identifier |
doi:10.1038/351371a0
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