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- W2000772738 abstract "On the basis of amino acid sequence homologies with other phospholipases C, the alpha-toxin of Clostridium perfringens was predicted to be a two-domain protein. Using truncated forms of alpha-toxin the phospholipase C active site was shown to be located in the amino-terminal domain. Crystallographic studies have confirmed this organisation and have also revealed that the carboxy-terminal domain is structurally similar to the phospholipid-binding domains in eukaryotic proteins. This information has been used to devise a model predicting how alpha-toxin interacts with membranes via calcium-mediated recognition of phospholipid head groups and the interaction of hydrophobic amino acids with the phospholipid tail group. The binding of alpha-toxin to membranes appears to result in the opening of the active site allowing hydrolysis of membrane phospholipids." @default.
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- W2000772738 date "2000-10-01" @default.
- W2000772738 modified "2023-10-16" @default.
- W2000772738 title "Opening of the active site of Clostridium perfringens α-toxin may be triggered by membrane binding" @default.
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- W2000772738 doi "https://doi.org/10.1016/s1438-4221(00)80040-5" @default.
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