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Title
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Crystal structure of a cholera toxin-related heat-labile enterotoxin from E. coli.
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Authors
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T.K.Sixma,
S.E.Pronk,
K.H.Kalk,
E.S.Wartna,
B.A.van Zanten,
B.Witholt,
W.G.Hol.
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Ref.
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Nature, 1991,
351,
371-377.
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PubMed id
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Abstract
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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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