Uedaira H, Morii H, Ishimura M, Taniguchi H, Namba K, Vonderviszt F
National Institute of Bioscience and Human-Technology, Tsukuba, Japan.
FEBS Lett. 1999 Feb 19;445(1):126-30. doi: 10.1016/s0014-5793(99)00110-6.
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.
