6CSM

Crystal structure of the natural light-gated anion channel GtACR1

6CSM の概要

• エントリーDOI: 10.2210/pdb6csm/pdb
• 分子名称: GtACR1, RETINAL, OLEIC ACID, ... (4 entities in total)
• 機能のキーワード: rhodopsin, channelrhodopsin, anion channel, optogenetics, membrane protein
• 由来する生物種: Guillardia theta CCMP2712
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 127789.57

構造登録者

Kato, H.E.,Kim, Y.,Yamashita, K.,Kobilka, B.K.,Deisseroth, K. (登録日: 2018-03-21, 公開日: 2018-09-05, 最終更新日: 2024-10-30)

主引用文献

Kato, H.E.,Kim, Y.S.,Paggi, J.M.,Evans, K.E.,Allen, W.E.,Richardson, C.,Inoue, K.,Ito, S.,Ramakrishnan, C.,Fenno, L.E.,Yamashita, K.,Hilger, D.,Lee, S.Y.,Berndt, A.,Shen, K.,Kandori, H.,Dror, R.O.,Kobilka, B.K.,Deisseroth, K.
Structural mechanisms of selectivity and gating in anion channelrhodopsins.
Nature, 561:349-354, 2018

PubMed Abstract: Both designed and natural anion-conducting channelrhodopsins (dACRs and nACRs, respectively) have been widely applied in optogenetics (enabling selective inhibition of target-cell activity during animal behaviour studies), but each class exhibits performance limitations, underscoring trade-offs in channel structure-function relationships. Therefore, molecular and structural insights into dACRs and nACRs will be critical not only for understanding the fundamental mechanisms of these light-gated anion channels, but also to create next-generation optogenetic tools. Here we report crystal structures of the dACR iC++, along with spectroscopic, electrophysiological and computational analyses that provide unexpected insights into pH dependence, substrate recognition, channel gating and ion selectivity of both dACRs and nACRs. These results enabled us to create an anion-conducting channelrhodopsin integrating the key features of large photocurrent and fast kinetics alongside exclusive anion selectivity.

PubMed: 30158697
DOI: 10.1038/s41586-018-0504-5

実験手法

X-RAY DIFFRACTION (2.9 Å)