Structural basis of ATP hydrolysis mechanism of V1-ATPase motor
Project/Area Number |
23370047
|
Research Category |
Grant-in-Aid for Scientific Research (B)
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Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
Structural biochemistry
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Research Institution | Chiba University |
Principal Investigator |
MURATA Takeshi 千葉大学, 理学(系)研究科(研究院), 准教授 (80415322)
|
Co-Investigator(Kenkyū-buntansha) |
YAMATO Ichiro 東京理科大学, 基礎工学部, 教授 (70111458)
|
Co-Investigator(Renkei-kenkyūsha) |
SAIJO Shinya 東京理科大学, 基礎工学部, 助教 (80419001)
MIZUTANI Kenji 東京理科大学, 基礎工学部, 博士研究員 (10525570)
|
Project Period (FY) |
2011-04-01 – 2014-03-31
|
Project Status |
Completed (Fiscal Year 2013)
|
Budget Amount *help |
¥14,950,000 (Direct Cost: ¥11,500,000、Indirect Cost: ¥3,450,000)
Fiscal Year 2013: ¥2,470,000 (Direct Cost: ¥1,900,000、Indirect Cost: ¥570,000)
Fiscal Year 2012: ¥2,470,000 (Direct Cost: ¥1,900,000、Indirect Cost: ¥570,000)
Fiscal Year 2011: ¥10,010,000 (Direct Cost: ¥7,700,000、Indirect Cost: ¥2,310,000)
|
Keywords | 分子モーター / 酵素反応 / V-ATPase / X線結晶構造解析 / ATP |
Research Abstract |
Vacuolar ATPases (V-ATPases) function as proton pumps in various membrane systems within the cells, which are involved in a number of processes such as bone resorption and cancer metastasis. The hydrophilic V1 portion is known as a rotary motor, in which a central axis DF complex rotates inside a hexagonally arranged catalytic A3B3 complex using ATP hydrolysis energy, although the molecular mechanism is not well defined due to a lack of high-resolution structural information. We have established the in vitro expression, purification, and reconstitution of Enterococcus hirae V1-ATPase from the A3B3 and DF complexes. In this study, we solved the crystal structures of AMP-PNP-bound and Pi-bound V1-ATPase, and also characterized the several site-directed mutants. On the basis of these findings, we proposed the molecular mechanism of the rotary motor.
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Report
(4 results)
Research Products
(42 results)
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[Journal Article] Mutant LV476-7AA of A-subunit of Enterococcus hirae V 1-ATPase : High affinity of A3B3 complex to DF axis and low ATPase activity2013
Author(s)
Md. Jahangir Alam, Ichiro Yamato, Satoshi Arai, Shinya Saijo, Kenji Mizutani, Yoshiko Ishizuka-Katsura, Noboru Ohsawa, Takaho Terada, Mikako Shirouzu, Shigeyuki Yokoyama, So Iwata, Yoshimi Kakinuma and Takeshi Murata
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Journal Title
SpringerPlus
Volume: 2
Pages: 689-689
Related Report
Peer Reviewed
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[Journal Article] Basic properties of rotary dynamics of the molecular motor Enterococcus hirae V1-ATPase2013
Author(s)
Yoshihiro Minagawa, Hiroshi Ueno, Mayu Hara, Yoshiko Ishizuka-Katsura, Noboru Ohsawa,Takaho Terada, Mikako Shirouzu, Shigeyuki Yokoyama, Ichiro Yamato, Eiro Muneyuki, Hiroyuki Noji, Takeshi Murata, and Ryota Iino
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Journal Title
J.Biol.Chem
Volume: 288
Issue: 45
Pages: 32700-32707
DOI
Related Report
Peer Reviewed
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[Journal Article] Loose Binding of the DF Axis with the A 3B3 Complex Stimulates the Initial Activity of Enterococcus hirae V 1-ATPase2013
Author(s)
Md. Jahangir Alam, Satoshi Arai, Shinya Saijo, Kano Suzuki, Kenji Mizutani, Yoshiko Ishizuka-Katsura, Noboru Ohsawa, Takaho Terada, Mikako Shirouzu, Shigeyuki Yokoyama, So Iwata, Yoshimi Kakinuma, Ichiro Yamato and Takeshi Murata
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Journal Title
PLoS ONE
Volume: 8
Issue: 9
Pages: e74291-e74291
DOI
Related Report
Peer Reviewed
-
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[Journal Article] Rotation mechanism of Enterococcus hirae V 1-ATPase based on asymmetric crystal structures2013
Author(s)
Satoshi Arai, Shinya Saijo, Kano Suzuki, Kenji Mizutani, Yoshimi Kakinuma, Yoshiko Ishizuka-Katsura, Noboru, Ohsawa, Takaho Terada, Mikako Shirouzu, Shigeyuki Yokoyama, So Iwata, Ichiro Yamato and Takeshi Murata
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Journal Title
Nature
Volume: 493
Issue: 7434
Pages: 703-707
DOI
Related Report
Peer Reviewed
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[Journal Article] Mutant LV476-7AA of A-subunit of Enterococcus hirae V1-ATPase: High affinity of A3B3 complex to DF axis and low ATPase activity2013
Author(s)
Md. Jahangir Alam, Ichiro Yamato, Satoshi Arai, Shinya Saijo, Kenji Mizutani, Yoshiko Ishizuka-Katsura, Noboru Ohsawa, Takaho Terada, Mikako Shirouzu, Shigeyuki Yokoyama, So Iwata, Yoshimi Kakinuma and Takeshi Murata
-
Journal Title
SpringerPlus
Volume: 2
Pages: 689-689
Related Report
Peer Reviewed
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