| アイテムタイプ |
学術雑誌論文 / Journal Article(1) |
| 公開日 |
2024-12-19 |
| タイトル |
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タイトル |
Multistep conformational changes leading to the gate opening of light-driven sodium pump rhodopsin |
| 言語 |
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言語 |
eng |
| キーワード |
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主題Scheme |
Other |
|
主題 |
membrane transport |
| キーワード |
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主題Scheme |
Other |
|
主題 |
sodium transport |
| キーワード |
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主題Scheme |
Other |
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主題 |
sodium pump |
| キーワード |
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主題Scheme |
Other |
|
主題 |
photobiology |
| キーワード |
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主題Scheme |
Other |
|
主題 |
rhodopsin |
| キーワード |
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|
主題Scheme |
Other |
|
主題 |
ion pump |
| キーワード |
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主題Scheme |
Other |
|
主題 |
retinal proteins |
| 資源タイプ |
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資源タイプ |
journal article |
| アクセス権 |
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アクセス権 |
open access |
| 著者 |
Sato, Yukino
Hashimoto, Tsubasa
Kato, Koji
Okamura, Akiko
Hasegawa, Kaito
Shinone, Tsukasa
Tanaka, Yoshikazu
Tanaka, Yoshiki
塚崎, 智也
Tsukamoto, Takashi
Demura, Makoto
Yao, Min
Kikukawa, Takashi
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| 抄録 |
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内容記述タイプ |
Abstract |
|
内容記述 |
Membrane transport proteins require a gating mechanism that opens and closes the substrate transport pathway to carry out unidirectional transport. The "gating" involves large conformational changes and is achieved via multistep reactions. However, these elementary steps have not been clarified for most transporters due to the difficulty of detecting the individual steps. Here, we propose these steps for the gate opening of the bacterial Na+ pump rhodopsin, which outwardly pumps Na+ upon illumination. We herein solved an asymmetric dimer structure of Na+ pump rhodopsin from the bacterium Indibacter alkaliphilus. In one protomer, the Arg108 sidechain is oriented toward the protein center and appears to block a Na+ release pathway to the extracellular (EC) medium. In the other protomer, however, this sidechain swings to the EC side and then opens the release pathway. Assuming that the latter protomer mimics the Na+-releasing intermediate, we examined the mechanism for the swing motion of the Arg108 sidechain. On the EC surface of the first protomer, there is a characteristic cluster consisting of Glu10, Glu159, and Arg242 residues connecting three helices. In contrast, this cluster is disrupted in the second protomer. Our experimental results suggested that this disruption is a key process. The cluster disruption induces the outward movement of the Glu159-Arg242 pair and simultaneously rotates the seventh transmembrane helix. This rotation resultantly opens a space for the swing motion of the Arg108 sidechain. Thus, cluster disruption might occur during the photoreaction and then trigger sequential conformation changes leading to the gate-open state. |
| 書誌情報 |
en : Journal of Biological Chemistry
巻 299,
号 12,
発行日 2023-10-27
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| 出版者 |
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出版者 |
Elsevier |
| ISSN |
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収録物識別子タイプ |
EISSN |
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収録物識別子 |
1083-351X |
| 出版者版DOI |
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関連タイプ |
isReplacedBy |
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識別子タイプ |
DOI |
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関連識別子 |
https://doi.org/10.1016/j.jbc.2023.105393 |
| 出版者版URI |
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関連タイプ |
isReplacedBy |
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識別子タイプ |
URI |
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関連識別子 |
https://www.sciencedirect.com/science/article/pii/S0021925823024213 |
| 権利 |
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|
権利情報Resource |
http://creativecommons.org/licenses/by/4.0/ |
|
権利情報 |
$00A9 2023 The Authors. Published by Elsevier Inc on behalf of American Society for Biochemistry and Molecular Biology. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/). |
| 著者版フラグ |
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出版タイプ |
NA |
