Abstract
Clostridium perfringens enterotoxin（CPE）is a cause of food poisoning and is considered a pore-forming toxin which damages target cells by disrupting the selective permeability of the plasma membrane. We determined the crystal structure of the full-length CPE at 2.0 Å. The overall structure of CPE displays an elongated shape, composed of three distinct domains, D1, D2, and D3. In this structure, the pore-forming domain（Val81〜Ile106）of CPE has alternating pattern of polar and hydrophobic residues and forms α-helix. This characteristic sequence is frequently observed in β pore-forming toxin families as typified by α-hemolysin. These results indicate that CPE behaves as β pore-forming toxins.
