Structural analysis of ion-bound state and transport mechanism of microbial rhodopsin by multinuclear solid-state NMR of microbial rhodopsins
| Project/Area Number |
18H02387
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Review Section |
Basic Section 43020:Structural biochemistry-related
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| Research Institution | Yokohama National University |
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Principal Investigator |
Kawamura Izuru 横浜国立大学, 大学院工学研究院, 准教授 (20452047)
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| Project Period (FY) |
2018-04-01 – 2021-03-31
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| Project Status |
Completed (Fiscal Year 2020)
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| Budget Amount *help |
¥17,550,000 (Direct Cost: ¥13,500,000、Indirect Cost: ¥4,050,000)
Fiscal Year 2020: ¥4,550,000 (Direct Cost: ¥3,500,000、Indirect Cost: ¥1,050,000)
Fiscal Year 2019: ¥5,330,000 (Direct Cost: ¥4,100,000、Indirect Cost: ¥1,230,000)
Fiscal Year 2018: ¥7,670,000 (Direct Cost: ¥5,900,000、Indirect Cost: ¥1,770,000)
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| Keywords | 固体NMR / レチナール / 化学シフト / イオン / 多核NMR / 膜タンパク質 / ロドプシン / イオン輸送 |
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| Outline of Final Research Achievements |
Membrane proteins play an important role in maintaining cell homeostasis. Among them, microbial rhodopsin is covalently bound to retinal chromophore via a protonated Schiff base, and the protein is activated by photo-isomerization. Solid-state NMR spectroscopy with multinuclear observations as well as 13C and 15N was applied to detect important interactions containing ion-bound states, contacts with water molecules, and aromatic stacking. It is found that monitoring of the alterations in NMR signals can find local structural change of microbial rhodopsin depending on pH, replacement of alkali metal ions, H/D exchange and point mutation. Furthermore, we developed a methodology such as In-situ microwave irradiation NMR method to investigate the non-thermal effects on polar group in a molecule.
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| Academic Significance and Societal Importance of the Research Achievements |
膜タンパク質の反応中心における特定の水素結合や静電的な相互作用などは膜タンパク質の重要な相互作用として特徴付けられ、分子レベルでそれらの機能を理解するためのアプローチとなる。そのような相互作用に対して、構造生物化学の分野で頻繁に利用される1H, 13C, 15N核以外にも多核的な観測によって、さらに深くアプローチできることを示した。今後、微生物型ロドプシンをはじめとした多くの膜タンパク質の動的構造の解明に活用できるものと期待できる。
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Report
(4 results)
Research Products
(64 results)
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[Journal Article] Structural determination of the sheath of Sphaerotilus montanus using thiopeptidoglycan lyase which cleaves the 1,4 linkage between α-D-GalN and β-D-GlcA2021
Author(s)
1. D. Kasiwabara, K. Kondo, R. Usami, D. Kan, I. Kawamura, Y. Kawasaki, M. Sato, T. Nittami, I. Suzuki, M. Katahira, M. Takeda
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Journal Title
International Journal of Biological Macromolecules
Volume: 183
Pages: 992-1001
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Peer Reviewed
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[Presentation] 多次元固体NMRによる細胞膜中のヘリオロドプシンの構造解析2019
Author(s)
鈴木 しぶき, 長島 敏雄, 金子 莉奈, 沖津 貴志, 和田 昭盛, 小林 直宏, 山崎 俊夫, 吉住 玲, 井上 圭一, 神取 秀樹, 川村 出
Organizer
第57回日本生物物理学会年会, 宮崎
Related Report
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[Presentation] 多次元固体NMRによるヘリオロドプシンの構造解析2019
Author(s)
鈴木 しぶき, 長島 敏雄, 金子 莉奈, 沖津 貴志, 和田 昭盛, 小林 直宏, 山崎 俊夫, 吉住 玲, 井上 圭一, 神取 秀樹, 川村 出
Organizer
第58回NMR討論会, 川崎
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[Presentation] Stereochemistry-dependent nanostructure of phenylalanine-based tripeptide self-assembly2018
Author(s)
◯Yumi Ozawa, Hisako Sato, Nana Yamaki, Yuichiro Izao, Atsumi Miyake, Akira Naito, Izuru Kawamura
Organizer
Asian Pacific Prion Symposium 2018 (APPS2018), Tokyo Metropolitan Industrial Technology Research Institute, Japan, Oct. 4-5, 2018. (Poster)
Related Report
Int'l Joint Research
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[Presentation] Membrane interactions of a D-amino acid containing antimicrobial peptides as revealed by experimental and theoretical methods2018
Author(s)
◯Batsaikhan Mijiddorj, Shiho Kaneda, Hisako Sato, Yuta Matsuo, Namsrai Javkhlantugs, Akira Naito, Kazuyoshi Ueda Izuru Kawamura
Organizer
The 10th International Peptide Symposium, ROHM theater, Kyoto, Dec. 3-7, 2018. (Poster)
Related Report
Int'l Joint Research
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