ID | 63078 |
フルテキストURL | |
著者 |
Tsujimura, Masaki
Department of Applied Chemistry, The University of Tokyo
Kojima, Keiichi
Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University
ORCID
Kaken ID
researchmap
Kawanishi, Shiho
Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University
Sudo, Yuki
Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University
ORCID
Kaken ID
researchmap
Ishikita, Hiroshi
Department of Applied Chemistry, The University of Tokyo
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抄録 | Anion channelrhodopsin from Guillardia theta (GtACR1) has Asp234 (3.2 angstrom) and Glu68 (5.3 angstrom) near the protonated Schiff base. Here, we investigate mutant GtACR1s (e.g., E68Q/D234N) expressed in HEK293 cells. The influence of the acidic residues on the absorption wavelengths was also analyzed using a quantum mechanical/molecular mechanical approach. The calculated protonation pattern indicates that Asp234 is deprotonated and Glu68 is protonated in the original crystal structures. The D234E mutation and the E68Q/D234N mutation shorten and lengthen the measured and calculated absorption wavelengths, respectively, which suggests that Asp234 is deprotonated in the wild-type GtACR1. Molecular dynamics simulations show that upon mutation of deprotonated Asp234 to asparagine, deprotonated Glu68 reorients toward the Schiff base and the calculated absorption wavelength remains unchanged. The formation of the proton transfer pathway via Asp234 toward Glu68 and the disconnection of the anion conducting channel are likely a basis of the gating mechanism.
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発行日 | 2021-12-21
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出版物タイトル |
Elife
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巻 | 10巻
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出版者 | eLIFE SCIENCES PUBL LTD
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開始ページ | e72264
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ISSN | 2050-084X
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資料タイプ |
学術雑誌論文
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言語 |
英語
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OAI-PMH Set |
岡山大学
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著作権者 | © Tsujimura et al.
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論文のバージョン | publisher
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PubMed ID | |
DOI | |
Web of Science KeyUT | |
関連URL | isVersionOf https://doi.org/10.7554/eLife.72264
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ライセンス | https://creativecommons.org/licenses/by/4.0/
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Citation | eLife 2021;10:e72264 DOI: 10.7554/eLife.72264
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