7C86

Time-resolved serial femtosecond crystallography reveals early structural changes in channelrhodopsin: Dark state structure

7C86 の概要

• エントリーDOI: 10.2210/pdb7c86/pdb
• 分子名称: Sensory opsin A,Channelrhodopsin (ChR) chimera between ChR1 & ChR2, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, RETINAL, ... (5 entities in total)
• 機能のキーワード: channelrhodopsin, rhodopsin, membrane protein
• 由来する生物種: Chlamydomonas reinhardtii; 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 43610.39

構造登録者

Oda, K.,Nomura, T.,Nakane, T.,Yamashita, K.,Inoue, K.,Ito, S.,Vierock, J.,Hirata, K.,Maturana, A.D.,Katayama, K.,Ikuta, T.,Ishigami, I.,Izume, T.,Umeda, R.,Eguma, R.,Oishi, S.,Kasuya, G.,Kato, T.,Kusakizako, T.,Shihoya, W.,Shimada, H.,Takatsuji, T.,Takemoto, M.,Taniguchi, R.,Tomita, A.,Nakamura, R.,Fukuda, M.,Miyauchi, H.,Lee, Y.,Nango, E.,Tanaka, R.,Tanaka, T.,Sugahara, M.,Kimura, T.,Shimamura, T.,Fujiwara, T.,Yamanaka, Y.,Owada, S.,Joti, Y.,Tono, K.,Ishitani, R.,Hayashi, S.,Kandori, H.,Hegemann, P.,Iwata, S.,Kubo, M.,Nishizawa, T.,Nureki, O. (登録日: 2020-05-28, 公開日: 2021-04-07, 最終更新日: 2024-10-23)

主引用文献

Oda, K.,Nomura, T.,Nakane, T.,Yamashita, K.,Inoue, K.,Ito, S.,Vierock, J.,Hirata, K.,Maturana, A.D.,Katayama, K.,Ikuta, T.,Ishigami, I.,Izume, T.,Umeda, R.,Eguma, R.,Oishi, S.,Kasuya, G.,Kato, T.,Kusakizako, T.,Shihoya, W.,Shimada, H.,Takatsuji, T.,Takemoto, M.,Taniguchi, R.,Tomita, A.,Nakamura, R.,Fukuda, M.,Miyauchi, H.,Lee, Y.,Nango, E.,Tanaka, R.,Tanaka, T.,Sugahara, M.,Kimura, T.,Shimamura, T.,Fujiwara, T.,Yamanaka, Y.,Owada, S.,Joti, Y.,Tono, K.,Ishitani, R.,Hayashi, S.,Kandori, H.,Hegemann, P.,Iwata, S.,Kubo, M.,Nishizawa, T.,Nureki, O.
Time-resolved serial femtosecond crystallography reveals early structural changes in channelrhodopsin.
Elife, 10:-, 2021

PubMed Abstract: Channelrhodopsins (ChRs) are microbial light-gated ion channels utilized in optogenetics to control neural activity with light . Light absorption causes retinal chromophore isomerization and subsequent protein conformational changes visualized as optically distinguished intermediates, coupled with channel opening and closing. However, the detailed molecular events underlying channel gating remain unknown. We performed time-resolved serial femtosecond crystallographic analyses of ChR by using an X-ray free electron laser, which revealed conformational changes following photoactivation. The isomerized retinal adopts a twisted conformation and shifts toward the putative internal proton donor residues, consequently inducing an outward shift of TM3, as well as a local deformation in TM7. These early conformational changes in the pore-forming helices should be the triggers that lead to opening of the ion conducting pore.

PubMed: 33752801
DOI: 10.7554/eLife.62389

実験手法

X-RAY DIFFRACTION (2.3 Å)