ArticleeLife2021
Time-resolved serial femtosecond crystallography reveals early structural changes in channelrhodopsin.
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Article in eLife, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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33citing papers in PubMed
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33 citing papers in PubMed, 74 citations in OpenAlex.
- Molecular mechanism of calcium inhibition in viral channelrhodopsins.Nature communications · 2026Article
- Val109 and Ile170 contribute to channel function in Guillardia theta-derived anion channelrhodopsins.Scientific reports · 2026Article
- Ferritinophagy in cardiovascular diseases: mechanisms and potential therapy.Molecular and cellular biochemistry · 2025Review
- Structure Determination from Single-Molecule X-ray Scattering Images Using Stochastic Gradient Ascent.Journal of chemical theory and computation · 2025Article
- A second photoactivatable state of the anion-conducting channelrhodopsin GtACR1 empowers persistent activity.Communications biology · 2025Article
- Ion-conducting and gating molecular mechanisms of channelrhodopsin revealed by true-atomic-resolution structures of open and closed states.Nature structural & molecular biology · 2025Article
- Deprotonation of retinal Schiff base and structural dynamics in the early photoreaction of primate blue cone visual pigment.Biophysical journal · 2025Article
- Pore-Opening and Ion-Conduction Mechanism in Channelrhodopsins C1C2, ChR2, and iChloC by Computational Electrophysiology and Constant-pH Simulations.Journal of chemical information and modeling · 2025Article
- Structural insights into light-gating of potassium-selective channelrhodopsin.Nature communications · 2025Article
- Structural Insights Into the Opening Mechanism of C1C2 Channelrhodopsin.Journal of the American Chemical Society · 2025Article
- Structural effects of high laser power densities on an early bacteriorhodopsin photocycle intermediate.Nature communications · 2024Article
- Bayesian electron density determination from sparse and noisy single-molecule X-ray scattering images.Science advances · 2024Article
- Identifying protein conformational states in the Protein Data Bank: Toward unlocking the potential of integrative dynamics studies.Structural dynamics (Melville, N.Y.) · 2024Article
- The time revolution in macromolecular crystallography.Structural dynamics (Melville, N.Y.) · 2024Article
- Metadynamics simulations reveal mechanisms of Na+ and Ca2+ transport in two open states of the channelrhodopsin chimera, C1C2.PloS one · 2024Article
- Emerging Time-Resolved X-Ray Diffraction Approaches for Protein Dynamics.Annual review of biophysics · 2023Review
- Structural mechanism of microbial rhodopsins: Report for the session 4 at the 19Biophysics and physicobiology · 2023Article
- Potassium-selective channelrhodopsins.Biophysics and physicobiology · 2023Article
- The Mechanism of the Channel Opening in Channelrhodopsin-2: A Molecular Dynamics Simulation.International journal of molecular sciences · 2023Article
- Properties of a Single Amino Acid Residue in the Third Transmembrane Domain Determine the Kinetics of Ambient Light-Sensitive Channelrhodopsin.International journal of molecular sciences · 2023Article
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Authors and funding
48 authors at 13 institutions in 3 countries.
Kazumasa Oda *Department of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo, Japan.ORCID 0000-0003-0996-0393
Takashi Nomura *Graduate School of Life Science, University of Hyogo, Hyogo, Japan.
Takanori Nakane *Department of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo, Japan.ORCID 0000-0003-2697-2767
Keitaro Yamashita *Department of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo, Japan.
Keiichi InoueGraduate School of Engineering, Nagoya Institute of Technology, Nagoya, Japan.ORCID 0000-0002-6898-4347
Shota ItoGraduate School of Engineering, Nagoya Institute of Technology, Nagoya, Japan.
Johannes VierockInstitute of Biology, Experimental Biophysics, Humboldt-Universität zu Berlin, Berlin, Germany.ORCID 0000-0001-7368-5539
Kunio HirataRIKEN SPring-8 Center, Hyogo, Japan.
Andrés D MaturanaDepartment of Bioengineering Sciences, Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya, Japan.
Kota KatayamaGraduate School of Engineering, Nagoya Institute of Technology, Nagoya, Japan.
Tatsuya IkutaDepartment of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo, Japan.
Itsuki IshigamiDepartment of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo, Japan.
Tamaki IzumeDepartment of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo, Japan.
Rie UmedaDepartment of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo, Japan.
Ryuun EgumaDepartment of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo, Japan.
Satomi OishiDepartment of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo, Japan.
Go KasuyaDepartment of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo, Japan.ORCID 0000-0003-1756-5764
Takafumi KatoDepartment of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo, Japan.
Tsukasa KusakizakoDepartment of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo, Japan.
Wataru ShihoyaDepartment of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo, Japan.
Hiroto ShimadaDepartment of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo, Japan.
Tomoyuki TakatsujiDepartment of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo, Japan.
Mizuki TakemotoDepartment of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo, Japan.ORCID 0000-0002-6339-6431
Reiya TaniguchiDepartment of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo, Japan.
Atsuhiro TomitaDepartment of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo, Japan.
Ryoki NakamuraDepartment of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo, Japan.
Masahiro FukudaDepartment of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo, Japan.
Hirotake MiyauchiDepartment of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo, Japan.
Yongchan LeeDepartment of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo, Japan.
Eriko NangoRIKEN SPring-8 Center, Hyogo, Japan.ORCID 0000-0001-9851-7355
Rie TanakaRIKEN SPring-8 Center, Hyogo, Japan.
Tomoyuki TanakaRIKEN SPring-8 Center, Hyogo, Japan.
Michihiro SugaharaRIKEN SPring-8 Center, Hyogo, Japan.
Tetsunari KimuraDepartment of Chemistry, Graduate School of Science, Kobe University, Kobe, Japan.
Tatsuro ShimamuraDepartment of Cell Biology, Graduate School of Medicine, Kyoto University, Kyoto, Japan.
Takaaki FujiwaraDepartment of Cell Biology, Graduate School of Medicine, Kyoto University, Kyoto, Japan.
Yasuaki YamanakaDepartment of Cell Biology, Graduate School of Medicine, Kyoto University, Kyoto, Japan.
Shigeki OwadaRIKEN SPring-8 Center, Hyogo, Japan.
Yasumasa JotiRIKEN SPring-8 Center, Hyogo, Japan.
Kensuke TonoRIKEN SPring-8 Center, Hyogo, Japan.
Ryuichiro IshitaniDepartment of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo, Japan.ORCID 0000-0002-4136-5685
Shigehiko HayashiDepartment of Chemistry, Graduate School of Science, Kyoto University, Kyoto, Japan.
Hideki KandoriGraduate School of Engineering, Nagoya Institute of Technology, Nagoya, Japan.
Peter HegemannInstitute of Biology, Experimental Biophysics, Humboldt-Universität zu Berlin, Berlin, Germany.ORCID 0000-0003-3589-6452
So IwataRIKEN SPring-8 Center, Hyogo, Japan.
Minoru KuboGraduate School of Life Science, University of Hyogo, Hyogo, Japan.
Tomohiro NishizawaDepartment of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo, Japan.ORCID 0000-0001-7463-8398
Osamu NurekiDepartment of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo, Japan.ORCID 0000-0003-1813-7008
The University of Tokyo · JPKyoto University · JPNagoya Institute of Technology · JPTohoku University · JPSPring-8 · JPHumboldt-Universität zu Berlin · DEJapan Science and Technology Agency · JPMRC Laboratory of Molecular Biology · GBUniversity of Hyogo · JPKobe University · JPMax Planck Institute of Biophysics · DENagoya University · JPPreferred Networks (Japan) · JP
Funding
Cluster of Excellence in Inflammation Research BIG-NSECluster of Excellence in Inflammation Research E4Cluster of Excellence in Inflammation Research SPP 1926Cluster of Excellence in Inflammation Research UniCatDeutsche Forschungsgemeinschaft SFB1078 (B2)European Research Council ERC-2016-StG 714762Hertie Foundation Senior Research ProfessorJapan Agency for Medical Research and Development Platform Project for Supporting Drug Discovery andLife Science Research (Basis for Supporting Innovative Drug Discovery and Life Science Research(BINDS))Japan Science and Technology Agency JPMJPR14L8Japan Science and Technology Agency JPMJPR14L9Japan Society for the Promotion of Science 16H06294Japan Society for the Promotion of Science 17H05000Japan Society for the Promotion of Science 18J21256Ministry of Education, Culture, Sports, Science and Technology X-ray Free-Electron Laser Priority Strategy Program
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.
Indexed as
Algal ProteinsAmino Acid SequenceChannelrhodopsinsChlamydomonas reinhardtiiCrystallographyIsomerismProtein ConformationProtein Structure, SecondarySequence AlignmentAlgal ProteinsChannelrhodopsinsC1C2channelrhodopsinchlamydomonas reinhardtiiChlamydomonas reinhardtiimolecular biophysicsstructural biology
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