2 0 0 0 OA 食中毒を引き起こすウェルシュ菌エンテロトキシンCPEの構造生物学的研究
- 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.
1 0 0 0 光回復酵素の結晶構造と補欠分子認識機構
- 著者
- 北所 健悟 三木 邦夫
- 出版者
- The Crystallographic Society of Japan
- 雑誌
- 日本結晶学会誌 (ISSN:03694585)
- 巻号頁・発行日
- vol.40, no.5, pp.322-328, 1998-10-28
The crystal structure of 8-HDF type photolyase from <I>Anacystis nidulans</I> showed the similarity of the backbone structure with MTHF type <I>E. coli</I> photolyase but completely different binding site of the light-harvesting cofactor. This is a first example that homologous primary and tertiary structures in closely related proteins recognize two different types of cofactors at different binding-sites. The structure and function of photolyase and its cofactor recoginition are reviewed and discussed.