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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Bacterial Toxins* / chemistry
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Bacterial Toxins* / metabolism
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Binding Sites
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Computer Graphics
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Crystallography
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Enterotoxins* / chemistry
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Enterotoxins* / metabolism
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Escherichia coli
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Escherichia coli Proteins*
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Gangliosides / metabolism
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Macromolecular Substances
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Models, Molecular
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Molecular Sequence Data
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NAD / metabolism
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Protein Conformation
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X-Ray Diffraction
Substances
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Bacterial Toxins
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Enterotoxins
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Escherichia coli Proteins
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Gangliosides
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Macromolecular Substances
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NAD
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heat-labile enterotoxin, E coli