2019 Fiscal Year Final Research Report
Structural analysis for vacuolar type ATPase to reveal molecular mechanism of rotary proton translocation
Project/Area Number |
17H03648
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Research Category |
Grant-in-Aid for Scientific Research (B)
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Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
Structural biochemistry
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Research Institution | Kyoto Sangyo University |
Principal Investigator |
YOKOYAMA Ken 京都産業大学, 生命科学部, 教授 (70271377)
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Co-Investigator(Kenkyū-buntansha) |
光岡 薫 大阪大学, 超高圧電子顕微鏡センター, 教授 (60301230)
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Project Period (FY) |
2017-04-01 – 2020-03-31
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Keywords | クライオ電子顕微鏡 / 構造解析 / 生体エネルギー変換 / V-ATPase / ATP合成 / エネルギー変換 / 分子モーター |
Outline of Final Research Achievements |
ATP synthase is an energy-converting molecular machine that converts the flow of protons through the membrane domain into rotational motion to synthesize ATP. In this study, the overall structure of V/A-type ATP synthase from thermophilic bacteria was clarified by single-particle analysis using cryo-electron microscopy. In addition, three rotation states were identified, enabled us to know motion of peripheral stalks during rotation. Then, the Vo portion was isolated and a density map of the atomic resolution was obtained by single-particle analysis using cryo electron microscope, indicating proton pathway from both sides of the membrane. Using these structures, we were able to construct an atomic model of the intact ATP synthase.
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Free Research Field |
生物物理学
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Academic Significance and Societal Importance of the Research Achievements |
クライオ電子顕微鏡による構造解析は、近年急速に発展した分野であり、生命現象を原子レベルで理解することを可能にする強力な手法である。また、タンパク質を標的とした薬剤設計に有効で、たとえばコロナウイルスの膜タンパク質に対する薬剤開発も可能にする。我々は、早い段階でこの手法に着目し、国内でははじめて複雑な膜タンパク質複合体の構造解析に成功し、この分野の進展に大きく貢献する成果となった。
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