Studies on molecular structure of metalloproteins
Project/Area Number |
24570163
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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 | Ehime University |
Principal Investigator |
SUGIURA Miwa 愛媛大学, プロテオサイエンスセンター, 准教授 (80312255)
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Project Period (FY) |
2012-04-01 – 2015-03-31
|
Project Status |
Completed (Fiscal Year 2014)
|
Budget Amount *help |
¥5,460,000 (Direct Cost: ¥4,200,000、Indirect Cost: ¥1,260,000)
Fiscal Year 2014: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2013: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
Fiscal Year 2012: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
|
Keywords | 金属タンパク質 / メタロチオネイン / 金属結合タンパク質複合体 |
Outline of Final Research Achievements |
Zinc ion is an essential element acting as a cofactor in more than 300 enzymes. However, high concentrations of Zn2+ are lethal for the cells. Thermophilic cyanobacterium, Thermosynechococcus elongatus, revealed higher resistance for Zn and Cd compared to other bacteria. In this study, we found that heavy-metal binding protein, metallothionein, in T. elongatus makes pentamer binding 50 atoms of Zn2+. Thus formation of multimer bound many Zn must be the reason of resistance to high concentration of Zn. Furthermore, we tried to analyse the molecular structure of this metallothionein by X-ray crystal structure. Although we obtained many crystals, the resolution was not high enough to know the molecular structure. Now, we are still working on cristallization for better resolution.
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Report
(4 results)
Research Products
(16 results)
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[Journal Article] Modification of the pheophytin redox potential in Thermosynechococcus elongatus Photosystem II with PsbA3 as D1.2014
Author(s)
Sugiura, M., Azami, C., Koyama, K., Rutherford, A. W., Rappaport, F., and Boussac, A.
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Journal Title
Biochim. Biophys. Acta (Bioenergetics)
Volume: 1837
Pages: 139-148
Related Report
Peer Reviewed
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[Journal Article] Evidence for an unprecedented histidine hydroxyl modification on D2-His336 in Photosystem II of Thermosynechoccocus vulcanus and Thermosynechoccocus elongatus2013
Author(s)
Sugiura, M., Koyama, K., Umena, Y., Kawakami, K., Shen, J.-R., Kamiya, N., and Boussac, A.
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Journal Title
Biochemistr
Volume: 52
Pages: 9427-9431
Related Report
Peer Reviewed
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[Journal Article] Environment of TyrZ in Photosystem II from Thermosynechococcus elongatus in which PsbA2 is the D1 protein2012
Author(s)
Sugiura, M., Ogami, S., Kusumi, M., Un, S., Rappaport, F., and Boussac, A.
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Journal Title
J. Biol. Chem.
Volume: 287
Pages: 13336-13347
Related Report
Peer Reviewed
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