2022 Fiscal Year Final Research Report
High resolution and dynamic structural analysis of the entire mammalian FoF1ATP synthase
| Project/Area Number |
19K15749
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| Research Category |
Grant-in-Aid for Early-Career Scientists
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| Allocation Type | Multi-year Fund |
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| Review Section |
Basic Section 38030:Applied biochemistry-related
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| Research Institution | Kyoto University |
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Principal Investigator |
Jiko Chimari 京都大学, 複合原子力科学研究所, 特別研究員(RPD) (70585976)
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| Project Period (FY) |
2019-04-01 – 2023-03-31
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| Keywords | Fo F1ATP合成酵素 / ミトコンドリア / 単粒子構造解析 |
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| Outline of Final Research Achievements |
Monomers, tetramers, and oligomers of mammalian mitochondrial FoF1ATP synthase, which are extremely unstable due to their flexibility with rotation, were stably purified without dissociation of subunits per form, and highly monodisperse cryogrids were successfully prepared. Single-particle structural analysis using cryo-electron microscopy led to a structure of the entire I F1-bound tetramer at approximately 7angstrom resolution.
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| Free Research Field |
構造生物学
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| Academic Significance and Societal Importance of the Research Achievements |
本研究は、ミトコンドリアの内膜に存在し、哺乳動物の生命活動を維持するために必要なATPエネルギーの95％以上を生産し、また近年の研究によってミトコンドリア膜透過性遷移孔（PTP）として機能することが明らかになってきているFoF1ATP 合成酵素の高分解能構造解析である。その詳細な構造は、本酵素が関与する疾患の創薬研究の基盤となる。
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