Elucidation of the molecular valve in the transporter to determine the direction of the transporter cycle
| Project/Area Number |
26460044
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Physical pharmacy
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| Research Institution | Toho University |
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Principal Investigator |
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| Co-Investigator(Kenkyū-buntansha) |
菊川 峰志 北海道大学, 先端生命科学研究院, 講師 (20281842)
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| Project Period (FY) |
2014-04-01 – 2017-03-31
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| Project Status |
Completed (Fiscal Year 2016)
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| Budget Amount *help |
¥5,070,000 (Direct Cost: ¥3,900,000、Indirect Cost: ¥1,170,000)
Fiscal Year 2016: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2015: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2014: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
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| Keywords | トランスポーター / 分子弁 / 水素結合ネットワーク / 輸送サイクル / 基質認識機構 / モジュレーター / 起電性輸送担体 |
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| Outline of Final Research Achievements |
To elucidate how the molecular valve can determine the direction of the transporter cycle in the transporter accompanying ion movement, we precisely determined the transports of human oligopeptide transporter (hPEPT1) and human Na+/monocarboxylate co-transporter (hSMCT1).
(1) We demonstrated using a chemical modification reagent for hydroxyl group, phenylmethylsulfonylfluoride (PMSF) that the hydroxyl group of Ser302 weakly forms the hydrogen-bonding with the imidazole of His57, which might keep the uptake activity optimum in the range of physiological intestinal pH.
(2) We elucidated with quantitative activity-structure relationship (QASR) that the molecular valve hSMCT1 might also determine the transport-direction of coupling Na+ ion and substrate.
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Report
(4 results)
Research Products
(29 results)
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[Journal Article] X-ray crystallographic structure of thermophilic rhodopsin: implications for high thermal stability and optogenetic function2016
Author(s)
Tsukamoto T, Mizutani K, Hasegawa T, Takahashi M, Honda N, Hashimoto N, Shimono K, Yamashita K, Yamamoto M, Miyauchi S, Takagi S, Hayashi S, Murata T, Sudo Y.
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Journal Title
J. Biol. Chem.
Volume: in press
Issue: 23
Pages: 12223-12232
DOI
Related Report
Peer Reviewed / Open Access / Acknowledgement Compliant
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[Journal Article] Structural basis for the slow photocycle and late proton release in Acetabularia rhodopsin I from the marine plant Acetabularia acetabulum2015
Author(s)
Furuse M, Tamogami J, Hosaka T, Kikukawa T, Shinya N, Hato M, Ohsawa N, Kim SY, Jung KH, Demura M, Miyauchi S, Kamo N, Shimono K,Kimura-Someya T, Yokoyama S, Shirouzu M
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Journal Title
Acta Crystallogr D Biol Crystallogr
Volume: 71
Issue: 11
Pages: 2203-2216
DOI
Related Report
Peer Reviewed / Open Access / Int'l Joint Research
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