2015年5月
Structural basis for Na+ transport mechanism by a light-driven Na+ pump
NATURE
- 巻
- 521
- 号
- 7550
- 開始ページ
- 48
- 終了ページ
- U347
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1038/nature14322
- 出版者・発行元
- NATURE PUBLISHING GROUP
Krokinobacter eikastus rhodopsin 2 (KR2) is the first light-driven Na+ pump discovered, and is viewed as a potential next-generation optogenetics tool. Since the positively charged Schiff base proton, located within the ion-conducting pathway of all light-driven ion pumps, was thought to prohibit the transport of a non-proton cation, the discovery of KR2 raised the question of how it achieves Na+ transport. Here we present crystal structures of KR2 under neutral and acidic conditions, which represent the resting and M-like intermediate states, respectively. Structural and spectroscopic analyses revealed the gating mechanism, whereby the flipping of Asp116 sequesters the Schiff base proton from the conducting pathway to facilitate Na+ transport. Together with the structure-based engineering of the first light-driven K1 pumps, electrophysiological assays in mammalian neurons and behavioural assays in a nematode, our studies reveal the molecular basis for light-driven non-proton cation pumps and thus provide a framework that may advance the development of next-generation optogenetics.
- リンク情報
- ID情報
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- DOI : 10.1038/nature14322
- ISSN : 0028-0836
- eISSN : 1476-4687
- PubMed ID : 25849775
- Web of Science ID : WOS:000354040900029