Study of structural basis of Na+ selective pump mechanism in Eh V-ATPase
| Project/Area Number |
16K07282
|
|---|
| Research Category |
Grant-in-Aid for Scientific Research (C)
|
| Allocation Type | Multi-year Fund |
|---|
| Section | 一般 |
|---|
| Research Field |
Structural biochemistry
|
|---|
| Research Institution | National Institute for Physiological Sciences |
|---|
Principal Investigator |
Murata Kazuyoshi 生理学研究所, 脳機能計測・支援センター, 准教授 (20311201)
|
|---|
| Research Collaborator |
MURATA Takeshi
UENO Hiroshi
IINO Ryota
|
|---|
| Project Period (FY) |
2016-04-01 – 2019-03-31
|
| Project Status |
Completed (Fiscal Year 2018)
|
| Budget Amount *help |
¥4,940,000 (Direct Cost: ¥3,800,000、Indirect Cost: ¥1,140,000)
Fiscal Year 2018: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2017: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2016: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
|
|---|
| Keywords | 膜タンパク質 / 回転式ATPase / クライオ電顕 / 低温電子顕微鏡 / 構造 / 蛋白質 |
|---|
| Outline of Final Research Achievements |
In this study, the structure of the entire V-ATPase (Eh V-ATPase), an ATP-driven sodium pump from Enterococcus hirae (Eh), was revealed by electron microscopy single particle analysis, and the selective ion transport mechanism was elucidated. It was found that in Eh V-ATPase, the rotor was bound to the off-center position of the rotating ring in the membrane. In addition, the major structural state of Eh V-ATPase was found to correspond to the minor structural state of the thermophilic bacterium V / A-ATPase. Furthermore, the mechanism by which Na+ is passed to the rotating c-ring is clarified.
|
| Academic Significance and Societal Importance of the Research Achievements |
本成果によって、Eh V-ATPaseのNa+輸送性のためのエネルギー伝達機構の構造基盤を明らかにすることができました。今後さらに詳細な構造研究を進めることによって、V-ATPaseが関係する疾患の治療法や治療薬の開発において重要な情報を提供することができると期待されます。
|
Report
(4 results)
Research Products
(15 results)
