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

by Kato, Takafumi , Hirata, Kunio , Miyauchi, Hirotake , Inoue, Keiichi , Shihoya, Wataru , Shimamura, Tatsuro , Nakane, Takanori , Takatsuji, Tomoyuki , Nureki, Osamu , Yamanaka, Yasuaki , Ito, Shota , Nishizawa, Tomohiro , Shimada, Hiroto , Takemoto, Mizuki , Ishitani, Ryuichiro , Nakamura, Ryoki , Tanaka, Tomoyuki , Yamashita, Keitaro , Tomita, Atsuhiro , Maturana, Andrés D , Owada, Shigeki , Nango, Eriko , Hayashi, Shigehiko , Fujiwara, Takaaki , Umeda, Rie , Ishigami, Itsuki , Kusakizako, Tsukasa , Kimura, Tetsunari , Oda, Kazumasa , Izume, Tamaki , Kasuya, Go , Taniguchi, Reiya , Katayama, Kota , Ikuta, Tatsuya , Oishi, Satomi , Hegemann, Peter , Sugahara, Michihiro , Lee, Yongchan , Kandori, Hideki , Tanaka, Rie , Joti, Yasumasa , Nomura, Takashi , Eguma, Ryuun , Iwata, So , Vierock, Johannes , Tono, Kensuke , Kubo, Minoru , Fukuda, Masahiro

in Analysis / C1C2 / Channel gating / Channel opening / channelrhodopsin / Chlamydomonas reinhardtii / Chromophores / Crystallography / Experiments / Free electron lasers / Genetics / Information processing / Intermediates / Ion channels / Isomerization / Optics / Photoactivation / Proteins / Retina / Spectrum analysis / Structural Biology and Molecular Biophysics

2021

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

2021

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

2021

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Journal Article

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

Kato, Takafumi,

Hirata, Kunio,

Miyauchi, Hirotake,

Inoue, Keiichi,

Shihoya, Wataru,

Shimamura, Tatsuro,

Nakane, Takanori,

Takatsuji, Tomoyuki,

Nureki, Osamu,

Yamanaka, Yasuaki,

Ito, Shota,

Nishizawa, Tomohiro,

Shimada, Hiroto,

Takemoto, Mizuki,

Ishitani, Ryuichiro,

Nakamura, Ryoki,

Tanaka, Tomoyuki,

Yamashita, Keitaro,

Tomita, Atsuhiro,

Maturana, Andrés D,

Owada, Shigeki,

Nango, Eriko,

Hayashi, Shigehiko,

Fujiwara, Takaaki,

Umeda, Rie,

Ishigami, Itsuki,

Kusakizako, Tsukasa,

Kimura, Tetsunari,

Oda, Kazumasa,

Izume, Tamaki,

Kasuya, Go,

Taniguchi, Reiya,

Katayama, Kota,

Ikuta, Tatsuya,

Oishi, Satomi,

Hegemann, Peter,

Sugahara, Michihiro,

Lee, Yongchan,

Kandori, Hideki,

Tanaka, Rie,

Joti, Yasumasa,

Nomura, Takashi,

Eguma, Ryuun,

Iwata, So,

Vierock, Johannes,

Tono, Kensuke,

Kubo, Minoru,

Fukuda, Masahiro

2021

Overview

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.

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Publisher

eLife Science Publications, Ltd,eLife Sciences Publications Ltd,eLife Sciences Publications, Ltd

Subject

/ C1C2

/ Chlamydomonas reinhardtii

/ Chromophores