7E6Y

Time-resolved serial femtosecond crystallography reveals early structural changes in channelrhodopsin: 1 microsecond structure

Summary for 7E6Y

• Entry DOI: 10.2210/pdb7e6y/pdb
• Descriptor: Archaeal-type opsin 1,Archaeal-type opsin 2, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, RETINAL, ... (5 entities in total)
• Functional Keywords: channelrhodopsin, rhodopsin, membrane protein
• Biological source: Chlamydomonas reinhardtii (Chlamydomonas smithii); More
• Total number of polymer chains: 1
• Total formula weight: 43610.39

Authors

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. (deposition date: 2021-02-24, release date: 2021-04-07, Last modification date: 2023-11-29)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.5 Å)