Abstract
Epsilon-toxin from Clostridium perfringens is a lethal toxin. Recent studies suggest that the toxin acts via an unusually potent pore-forming mechanism. Here we report the crystal structure of epsilon-toxin, which reveals structural similarity to aerolysin from Aeromonas hydrophila. Pore-forming toxins can change conformation between soluble and transmembrane states. By comparing the two toxins, we have identified regions important for this transformation.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Aeromonas / metabolism
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Amino Acid Sequence
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Bacillus / metabolism
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Bacterial Toxins / chemistry*
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Cell Membrane / metabolism
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Crystallography, X-Ray
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Models, Molecular
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Molecular Sequence Data
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Pore Forming Cytotoxic Proteins
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Protein Conformation
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Protein Structure, Tertiary
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Sequence Homology, Amino Acid
Substances
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Bacterial Toxins
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Clostridium perfringens epsilon-toxin
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Pore Forming Cytotoxic Proteins
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aerolysin