Domain organization of flagellar hook protein from Salmonella typhimurium

FEBS Letters

Ishimura, Miyuki²  Morii, Hisayuki²  Vonderviszt, Ferenc¹  Taniguchi, Hisaaki³  Namba, Keiichi¹  Uedaira, Hatsuho² 

[1] International Institute for Advanced Research, Matsushita Electric Industrial Co., Ltd., 3-4 Hikaridai, Seika 619-0237, Japan;National Institute of Bioscience and Human-Technology, 1-1 Higashi, Tsukuba 305-8566, Japan;Institute for Comprehensive Medical Science, Fujita Health University, Kutsukake-cho, Toyoake 470-1192, Japan

关键词: Bacterial flagellum;    Hook;    Domain structure;    Calorimetry;    Salmonella typhimurium;   

DOI  :  10.1016/S0014-5793(99)00110-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Hook forms a universal joint, which mediates the torque of the flagellar motor to the outer helical filaments. Domain organization of hook protein from Salmonella typhimurium was investigated by exploring thermal denaturation properties of its proteolytic fragments. The most stable part of hook protein involves residues 148 to 355 and consists of two domains, as revealed by deconvolution analysis of the calorimetric melting profiles. Residues 72–147 and 356–370 form another domain, while the terminal regions of the molecule, residues 1–71 and 371–403, avoid a compact tertiary structure in the monomeric state. These folding domains were assigned to the morphological domains of hook subunits known from EM image reconstructions, revealing the overall folding of hook protein in its filamentous state.

【 授权许可】

Unknown