| Co-Investigator(Kenkyū-buntansha) |
中川 敦史 大阪大学, たんぱく質研究所, 教授 (20188890)
藤原 祐一郎 大阪大学, 医学(系)研究科(研究院), 准教授 (20532980)
坂田 宗平 大阪大学, 医学(系)研究科(研究院), 招へい教員 (40528006)
筒井 秀和 大阪大学, 医学(系)研究科(研究院), 講師 (30392038)
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| Budget Amount *help |
¥46,020,000 (Direct Cost: ¥35,400,000、Indirect Cost: ¥10,620,000)
Fiscal Year 2015: ¥14,170,000 (Direct Cost: ¥10,900,000、Indirect Cost: ¥3,270,000)
Fiscal Year 2014: ¥14,170,000 (Direct Cost: ¥10,900,000、Indirect Cost: ¥3,270,000)
Fiscal Year 2013: ¥17,680,000 (Direct Cost: ¥13,600,000、Indirect Cost: ¥4,080,000)
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| Outline of Final Research Achievements |
Toward understanding general principle of domain-to-domain coupling in membrane proteins, we have exploited advantages of voltage-sensor domain proteins including voltage-gated proton channel (VSOP/Hv1) and voltage-sensing phosphatase. Approach of electrophysiology, voltage clamp fluorometery of cysteine-based method as well as fluorescent unnatural amino acid incorporation based on the genetic method enabled to reveal intermediate state of enzyme coupled to partially activated voltage sensor in VSP. X-ray crystal structure of voltage-gated proton channel was solved at 3.45 angstrom resolution as the zinc bound closed state, showing two S4 helices running straight next to each other within dimer in membrane which formed continuous helix down to the dimer cytoplasmic coiled coil at the C-terminus.
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