Understanding of the mechanisms of F1-ATPase by redesigning beta-subunit's P-loop
| Project/Area Number |
15H05592
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| Research Category |
Grant-in-Aid for Young Scientists (A)
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| Allocation Type | Single-year Grants |
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| Research Field |
Biophysics
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| Research Institution | Center for Novel Science Initatives, National Institutes of Natural Sciences (2018)
Institute for Molecular Science (2015-2017) |
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Principal Investigator |
KOGA Nobuyasu 大学共同利用機関法人自然科学研究機構(新分野創成センター、アストロバイオロジーセンター、生命創成探究, 生命創成探究センター, 准教授 (50432571)
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| Research Collaborator |
Koga Rie
Ueno Hiroshi
Noji Hiroyuki
Masaike Tomoko
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| Project Period (FY) |
2015-04-01 – 2019-03-31
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| Project Status |
Completed (Fiscal Year 2018)
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| 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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| Keywords | タンパク質分子デザイン / 分子モーター / F1-ATPase / 構造変化 / P-loop / 分子動力学シミュレーション / １分子回転計測実験 / 改造 / 分子シミュレーション / 計算機デザイン / 生化学実験 / 合理デザイン / 生物物理 / 分子モータータンパク質 / 計算機シミュレーション / シーソーモチーフ |
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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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| Academic Significance and Societal Importance of the Research Achievements |
F1-ATPaseはほぼ全ての生物が有し、生命のエネルギー源であるATPを合成する酵素である。F1の構造変化の仕組みを理解することは、生命の制御・設計という観点において、F1の構造変化、すなわちATP合成を制御する技術を構築する上で重要となる。また、F1-ATPaseの構造変化の仕組みを理解することで、蛋白質の構造変化原理の普遍的な理解と、さらには構造変化するタンパク質のデザイン原理の解明につながる。
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Report
(5 results)
Research Products
(13 results)
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[Presentation] Design of ideal protein structures2015
Author(s)
Nobuyasu Koga
Organizer
The 15th KIAS Conference on Protein Structure and Function, Korea Institute for Advanced Study
Place of Presentation
Seoul, Korea
Year and Date
2015-09-17
Related Report
Int'l Joint Research / Invited
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