| Budget Amount *help |
¥23,400,000 (Direct Cost: ¥18,000,000、Indirect Cost: ¥5,400,000)
Fiscal Year 2018: ¥5,720,000 (Direct Cost: ¥4,400,000、Indirect Cost: ¥1,320,000)
Fiscal Year 2017: ¥5,720,000 (Direct Cost: ¥4,400,000、Indirect Cost: ¥1,320,000)
Fiscal Year 2016: ¥5,070,000 (Direct Cost: ¥3,900,000、Indirect Cost: ¥1,170,000)
Fiscal Year 2015: ¥6,890,000 (Direct Cost: ¥5,300,000、Indirect Cost: ¥1,590,000)
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| Outline of Final Research Achievements |
F1-ATPase is a rotary molecular motor utilizing ATP as an energy source. In this study, we aimed to reveal the mechanisms of conformational change of the beta-subunit. On the basis of comparison of the beta-subunit with the alpha-subunit that does not change its conformation upon ATP binding, we hypothesized that the sequence difference in the xxxx region of P-loop (GxxxxGKT/S), a phosphate-binding motif, may play an important role for the conformational change. We investigated the impact of the sequence in the xxxx region on the conformational change by mutating the sequence from beta to alpha, performing molecular dynamics simulations, single-molecule experiments, etc. These results illuminate how the beta-subunit encodes its conformational change in the P-loop.
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