| Project/Area Number |
21570164
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Biophysics
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| Research Institution | Nagoya University |
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Principal Investigator |
IHARA Kunio 名古屋大学, 遺伝子実験施設, 助教 (90223297)
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| Co-Investigator(Kenkyū-buntansha) |
KOUYAMA Tsutomu 名古屋大学, 大学院・理学研究科, 教授 (30170210)
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| Project Period (FY) |
2009 – 2011
|
| Project Status |
Completed (Fiscal Year 2011)
|
| Budget Amount *help |
¥4,940,000 (Direct Cost: ¥3,800,000、Indirect Cost: ¥1,140,000)
Fiscal Year 2011: ¥910,000 (Direct Cost: ¥700,000、Indirect Cost: ¥210,000)
Fiscal Year 2010: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2009: ¥2,860,000 (Direct Cost: ¥2,200,000、Indirect Cost: ¥660,000)
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| Keywords | 光生物学 / 構造生物学 / エネルギー変換 / イオンポンプ / ハロロドプシン / 膜タンパク質 / 構造解析 / 古細菌 / 好塩菌 / 膜電位感受性 |
|---|
| Research Abstract |
An extremely haloalkaliphilic archaon Natronomonas pharaonis possesses the light-drivenchloride ion pump, halorhodopsin(pHR) on its membrane. We purified pHR in the form of native membrane, crystallized, and solved its structure at 2. 0A resolution. Furthermore we succeeded to solve the structure of chloride ion free blue form of pHR, which is considered to be O-like intermediate. From the structure comparison between chloride-boud and chloride-free forms of pHR, it was shown that the removal of the chloride ion, which is located between the retinal Schiff base and Thr126, is accompanied by such a deformation of helix C that the side chain of Thr126 moves toward helix G, leading to a significant shrinkage of the chloride ion binding site and the water molecule, which was hydrogen boded with the chloride ion, had moved.
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