- 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
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.