Article
Torque generation and utilization in motor enzyme F0F1-ATP synthase: half-torque F1 with short-sized pushrod helix and reduced ATP Synthesis by half-torque F0F1.
The Journal of biological chemistry - 13 Jan 2012
Usukura Eiji, Suzuki Toshiharu, Furuike Shou, Soga Naoki, Saita Ei-Ichiro, Hisabori Toru, Kinosita Kazuhiko, Yoshida Masasuke
Abstract excerpt
ATP synthase (F(0)F(1)) is made of two motors, a proton-driven motor (F(0)) and an ATP-driven motor (F(1)), connected by a common rotary shaft, and catalyzes proton flow-driven ATP synthesis and ATP-driven proton pumping. In F(1), the central γ subunit rotates inside the α(3)β(3) ring. Here we report structural features of F(1) responsible for torque generation and the catalytic ability of the low-torque...
Topics
- Adenosine Triphosphate
- Catalysis
- Catalytic Domain
- Escherichia coli
- Escherichia coli Proteins
- Helix-Loop-Helix Motifs
- Mutation
- Protein Structure, Tertiary
- Proton-Motive Force
- Proton-Translocating ATPases