Time-resolved serial femtosecond crystallography reveals early structural changes in channelrhodopsin

Autor: Tomoyuki Takatsuji, Tomoyuki Tanaka, Yasumasa Joti, Tomohiro Nishizawa, Satomi Oishi, Rie Umeda, Hiroto Shimada, Shigehiko Hayashi, Wataru Shihoya, Osamu Nureki, Rie Tanaka, Atsuhiro Tomita, Tetsunari Kimura, Peter Hegemann, Tatsuya Ikuta, Kunio Hirata, Takafumi Kato, Andrés D. Maturana, Kazumasa Oda, Yongchan Lee, Tamaki Izume, Reiya Taniguchi, Hideki Kandori, Masahiro Fukuda, Hirotake Miyauchi, Takashi Nomura, Kota Katayama, Keiichi Inoue, Minoru Kubo, Ryuun Eguma, So Iwata, Ryuichiro Ishitani, Keitaro Yamashita, Kensuke Tono, Eriko Nango, Takanori Nakane, Yasuaki Yamanaka, Ryoki Nakamura, Go Kasuya, Shota Ito, Shigeki Owada, Mizuki Takemoto, Tatsuro Shimamura, Tsukasa Kusakizako, Johannes Vierock, Michihiro Sugahara, Takaaki Fujiwara, Itsuki Ishigami
Jazyk: angličtina
Rok vydání: 2021
Předmět:
Zdroj: eLife, Vol 10 (2021)
eLife
Popis: 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.
X線自由電子レーザーを用いて、光照射によるチャネルロドプシンの構造変化の過程を捉えることに成功. 京都大学プレスリリース. 2021-03-26.
Databáze: OpenAIRE