A joint research group of Nagoya University, Nagaoka Bio University, and Yokohama National University has elucidated the structural dynamics of the FliG molecule, which is one of the proteins that make up the motor organ furrow motor of bacteria.
The rotary motor at the base of the bacterial flag is called the "bacterial motor", and although it is only 45 nanometers, it can rotate at an ultra-high speed comparable to the engine speed of an F1 machine.Furthermore, it is an extremely excellent motor that instantly changes the direction of rotation from the top speed and has an energy conversion efficiency of almost 100%.
Of the proteins that make up the rotor of a flagellar motor, FliG is known to interact with the stator and has been thought to play a major role in the rotational movement of the motor. Until now, the detailed molecular mechanism and interaction mode have not been elucidated.
This time, the group prepared amino acid variants of the C-terminal domain (FliGc) of FliG protein and aimed to elucidate the conversion control mechanism in the rotational direction by comparing with wild-type FliGc.As a result, FliGc mainly forms three conformations and has a dynamic property of moving back and forth between multiple structures, which plays an important role in determining forward and backward movements. It was revealed.
The characteristic dynamics found this time are expected to be important for converting the rotation direction of the motor with high energy conversion efficiency, and by artificially designing nanomachines based on this knowledge, medical and artificial life design It is expected to be applied to various fields such as.
Paper information:[Structure] Structural and functional analysis of C-terminal region of FliG, an essential motor component of Vibrio Na + -driven flagella
