Crystallization and structural analysis of proton motor of ATP synthase
| Project/Area Number |
19770103
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
Functional biochemistry
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| Research Institution | Tokyo Institute of Technology |
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Principal Investigator |
MITOME Noriyo Tokyo Institute of Technology, 物質工学科, 講師 (90431981)
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| Project Period (FY) |
2007 – 2010
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| Project Status |
Completed (Fiscal Year 2010)
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| Budget Amount *help |
¥4,080,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥780,000)
Fiscal Year 2010: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2009: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2008: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2007: ¥700,000 (Direct Cost: ¥700,000)
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| Keywords | ATP合成酵素 / 構造解析 / 分子モーター / プロトンポンプ |
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| Research Abstract |
In FoF1-ATP synthase that couples H+ transport with ATP synthesis/hydrolysis, an Foc subunit decamer ring (c-ring) rotates relative to F_oa as protons pass through Fo. To understand the torque generation mechanism, structural and functional information is required. In this study, I generated c_<10>-aF_oF_1 in which c_<10> and F_oa were genetically fused. The biochemical analysis revealed that the conserved arginine residue in F_oa ensures proton-coupled c-ring rotation by preventing a futile proton shortcut. I also successfully purified c_<10>-a F_o and analyzed stability of complexes for crystallization of F_o.
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Report
(6 results)
Research Products
(29 results)
