Thomas D R, Morgan D G, DeRosier D J
W. M. Keck Institute for Cellular Visualization, Rosenstiel Basic Medical Sciences Research Center, Department of Biology, Brandeis University, Waltham, MA 02254, USA.
Proc Natl Acad Sci U S A. 1999 Aug 31;96(18):10134-9. doi: 10.1073/pnas.96.18.10134.
FliG, FliM, and FliN, key proteins for torque generation, are located in two rings. The first protein is in the M ring and the last two are in the C ring. The rotational symmetries of the C and M rings have been determined to be about 34 (this paper) and 26 (previous work), respectively. The mechanism proposed here depends on the symmetry mismatch between the rings: the C ring extends 34 levers, of which 26 can bind to the 26 equivalent sites on the M ring. The remaining 8 levers bind to proton-pore complexes (studs) to form 8 torque generators. Movement results from the swapping of stud-bound levers with M ring-bound levers. The model predicts that both the M and C rings rotate in the same direction but at different speeds.
FliG、FliM和FliN是产生扭矩的关键蛋白,位于两个环中。第一种蛋白位于M环,后两种位于C环。已确定C环和M环的旋转对称性分别约为34(本文)和26(先前的研究)。这里提出的机制取决于环之间的对称性不匹配:C环伸出34个杠杆,其中26个可以与M环上的26个等效位点结合。其余8个杠杆与质子孔复合物(支柱)结合形成8个扭矩发生器。运动源于与支柱结合的杠杆与与M环结合的杠杆的交换。该模型预测M环和C环都沿相同方向旋转,但速度不同。