Structure basis for E2-E3 interation in plant Atg conjugation system
Project/Area Number |
25871076
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Research Category |
Grant-in-Aid for Young Scientists (B)
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Allocation Type | Multi-year Fund |
Research Field |
Structural biochemistry
Functional biochemistry
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Research Institution | Microbial Chemistry Research Foundation |
Principal Investigator |
MATOBA Kazuaki 公益財団法人微生物化学研究会, 微生物化学研究所, 研究員 (60613792)
|
Project Period (FY) |
2013-04-01 – 2015-03-31
|
Project Status |
Completed (Fiscal Year 2014)
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Budget Amount *help |
¥4,290,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥990,000)
Fiscal Year 2014: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2013: ¥2,470,000 (Direct Cost: ¥1,900,000、Indirect Cost: ¥570,000)
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Keywords | X線結晶構造解析 / オートファジー |
Outline of Final Research Achievements |
We identified the minimum binding region of Atg3 for Atg12 by in vitro pull-down assay using Arabidopsis thaliana (At) homologs and crystallized the AtAtg12b-AtAtg3 peptide complex. The side-chain of AtAtg3 Asp-Met is bound deeply to the pocket of AtAtg12b. The importance of AtAtg3 Met157 for AtAtg12b binding was confirmed by mutational analysis. These data establish the basis for E2-E3 interaction in the plant Atg system.
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Report
(3 results)
Research Products
(3 results)
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[Journal Article] Atg12-Atg5 conjugate enhances E2 activity of Atg3 by rearranging its catalytic site2013
Author(s)
Sakoh-Nakatogawa, M., Matoba, K., Asai, E., Kirisako, H., Ishii, J., Noda, N. N., Inagaki, F., Nakatogawa, H. and Ohsumi, Y
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Journal Title
Nature Structural & Molecular Biology
Volume: Vol.20
Issue: 4
Pages: 433-439
DOI
Related Report
Peer Reviewed
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