| Project/Area Number |
15K13744
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| Research Category |
Grant-in-Aid for Challenging Exploratory Research
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| Allocation Type | Multi-year Fund |
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| Research Field |
Bio-related chemistry
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| Research Institution | Nara Institute of Science and Technology |
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Principal Investigator |
HIROTA Shun 奈良先端科学技術大学院大学, 物質創成科学研究科, 教授 (90283457)
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| Co-Investigator(Renkei-kenkyūsha) |
HIGUCHI Yoshiki 兵庫県立大学, 大学院生命理学研究科, 教授 (90183574)
NAGAO Satoshi 奈良先端科学技術大学院大学, 物質創成科学研究科, 助教 (30452535)
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| Project Period (FY) |
2015-04-01 – 2017-03-31
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| Project Status |
Completed (Fiscal Year 2016)
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| Budget Amount *help |
¥3,900,000 (Direct Cost: ¥3,000,000、Indirect Cost: ¥900,000)
Fiscal Year 2016: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
Fiscal Year 2015: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
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| Keywords | タンパク質 / 生体分子 / ナノバイオ / 超分子化学 / タンパク質構造体 / タンパク質ケージ / ドメインスワッピング / 蛋白質 / 蛋白質構造体 / 蛋白質ケージ / 超分子 |
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| Outline of Final Research Achievements |
Cytochrome (cyt) cb562 oligomers were constructed, and it was found that the dimer of cyt cb562 forms a domain-swapped structure. Three domain-swapped cyt cb562 dimers formed a unique cage structure with a Zn-SO4 cluster inside the cavity. The Zn-SO4 cluster consisted of fifteen Zn2+ and seven SO42- ions, whereas six additional Zn2+ ions were detected inside the cavity. Fusion proteins comprising the subunits of different homo oligomeric proteins were designed. The two subunits were connected with a 3-helix bundle protein in the fusion proteins. A tetramer and a hexamer were constructed with the fusion proteins, and the structures of the tetramer and hexamer were analyzed by small-angle X-ray scattering and high-speed atomic force microscopy methods.
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