著者

北所 健悟 西村 昂亮 神谷 重樹 堀口 安彦

出版者

日本結晶学会

雑誌

日本結晶学会誌 (ISSN:03694585)

巻号頁・発行日

vol.55, no.3, pp.223-229, 2013-06-30 (Released:2013-07-02)

参考文献数

38

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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.