Activation and stiffness of the inhibited states of F1-ATPase probed by single-molecule manipulation.

@article{Saita2010ActivationAS,
  title={Activation and stiffness of the inhibited states of F1-ATPase probed by single-molecule manipulation.},
  author={Ei-ichiro Saita and Ryota Iino and Toshiharu Suzuki and Boris A Feniouk and Kazuhiko Kinosita and Masasuke Yoshida},
  journal={The Journal of biological chemistry},
  year={2010},
  volume={285 15},
  pages={11411-7}
}
F(1)-ATPase (F(1)), a soluble portion of F(o)F(1)-ATP synthase (F(o)F(1)), is an ATP-driven motor in which gammaepsilon subunits rotate in the alpha(3)beta(3) cylinder. Activity of F(1) and F(o)F(1) from Bacillus PS3 is attenuated by the epsilon subunit in an inhibitory extended form. In this study we observed ATP-dependent transition of epsilon in single F… CONTINUE READING