Article
The rotor tip inside a bearing of a thermophilic F1-ATPase is dispensable for torque generation.
Biophysical journal - 1 Jun 2006
Hossain Mohammad Delawar, Furuike Shou, Maki Yasushi, Adachi Kengo, Ali M Yusuf, Huq Mominul, Itoh Hiroyasu, Yoshida Masasuke, Kinosita Kazuhiko
Abstract excerpt
F(1)-ATPase is an ATP-driven rotary molecular motor in which the central gamma-subunit rotates inside a stator cylinder made of alpha(3)beta(3) subunits. To elucidate the role of rotor-stator interactions in torque generation, we truncated the gamma-subunit at its carboxyl terminus, which forms an alpha helix that penetrates deeply into the stator cylinder. We used an alpha(3)beta(3)gamma subcomplex of...
Topics
- Bacillus
- Catalytic Domain
- Models, Molecular
- Molecular Motor Proteins
- Mutation
- Protein Binding
- Protein Conformation
- Protein Subunits
- Proton-Translocating ATPases
- Recombinant Proteins
- Torque