Understanding of the regulatory mechanism on the activity of chloroplast-type ATP synthase by X-ray crystallography
Project/Area Number |
23570159
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Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Multi-year Fund |
Section | 一般 |
Research Field |
Functional biochemistry
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Research Institution | Kanazawa University |
Principal Investigator |
KONNO HIROKI 金沢大学, バイオAFM先端研究センター, 准教授 (80419267)
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Project Period (FY) |
2011 – 2013
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Project Status |
Completed (Fiscal Year 2013)
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Budget Amount *help |
¥5,330,000 (Direct Cost: ¥4,100,000、Indirect Cost: ¥1,230,000)
Fiscal Year 2013: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
Fiscal Year 2012: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
Fiscal Year 2011: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
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Keywords | ATP合成酵素 / 葉緑体 / 活性制御 / ATP合成酵素 |
Research Abstract |
Inserted region on the gamma subunit of chloroplast type ATP synthase strongly affect to the inhibitory effect of endogenous epsilon subunit (epsilon inhibition). To understand the relationship between the inserted region and the epsilon subunit, we try to dissolve structure of sub-complex of chloroplast type ATP synthase (alpha3beta3gamma1epsilon1). Though we could not yet get crystal in high resolution, we succeeded to make stable sub-complex mutant for crystallization and could get some crystal. We also investigated an affect of the inserted region on the gamma subunit to the ATPase activity on the beta subunit because these two parts exist far form each other. We then identified a conformational change of two central alpha helices in gamma subunit which is interact with catalytic sites on the beta subunit is necessary to read regulatory effect of the inserted region.
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Report
(4 results)
Research Products
(26 results)
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[Journal Article] Nano-scale alignment of proteins on a nexible DNA back-bone2012
Author(s)
Nojima, T.*, Konno, H., Kodera, N., Seio, K, Taguchi, H., Yoshida, M.
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Journal Title
PLoS One
Volume: 7
Issue: 12
Pages: 52534-52534
DOI
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Peer Reviewed
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[Journal Article] Regulation of F_oF_1-ATPase from Synechocystis sp. PCC 6803 by theγandεsubunits is significant for light/dark adaptation2011
Author(s)
Imashimizu, M., Bernat, G., Sunamura, EI., Broekmans, M., Konno, H., Isato, K., Roegner, M., Hisabori, T.
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Journal Title
J. Biol. Chem.
Volume: 286
Issue: 30
Pages: 26595-26602
DOI
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[Presentation] Conformational change of theγsubunit regulates the ATP hydrolysis activity of cyanobacterial ATP synthase2012
Author(s)
Sunamura, EI, Konno, H, Imashimizu, M, Mochimaru, M, Hisabori, T.
Organizer
17th European Bioenergetics Conference
Place of Presentation
University of Freiburg, Germany
Related Report
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[Presentation] Conformational change of the γ subunit regulates the ATP hydrolysis activity of cyanobacterial ATP synthase2012
Author(s)
Sunamura, EI, Konno, H, Imashimizu, M, Mochimaru, M, Hisabori, T
Organizer
17th European Bioenergetics Conference
Place of Presentation
University of Freiburg, Germany
Related Report
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