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Open data
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Basic information
| Entry | Database: PDB / ID: 5h3o | ||||||||||||||||||||||||||||||||||||||||||||||||
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| Title | Structure of a eukaryotic cyclic nucleotide-gated channel | ||||||||||||||||||||||||||||||||||||||||||||||||
Components | Cyclic nucleotide-gated cation channel | ||||||||||||||||||||||||||||||||||||||||||||||||
Keywords | TRANSPORT PROTEIN / TAX-4 / CNG / Channel / Open state | ||||||||||||||||||||||||||||||||||||||||||||||||
| Function / homology | Function and homology informationdetection of carbon dioxide / detection of chemical stimulus involved in sensory perception / Activation of the phototransduction cascade / Inactivation, recovery and regulation of the phototransduction cascade / VxPx cargo-targeting to cilium / ciliary inversin compartment / multicellular organismal reproductive process / thermosensory behavior / positive regulation of growth rate / G protein-coupled receptor signaling pathway coupled to cGMP nucleotide second messenger ...detection of carbon dioxide / detection of chemical stimulus involved in sensory perception / Activation of the phototransduction cascade / Inactivation, recovery and regulation of the phototransduction cascade / VxPx cargo-targeting to cilium / ciliary inversin compartment / multicellular organismal reproductive process / thermosensory behavior / positive regulation of growth rate / G protein-coupled receptor signaling pathway coupled to cGMP nucleotide second messenger / olfactory behavior / intracellular cyclic nucleotide activated cation channel complex / intracellularly cGMP-activated cation channel activity / aerotaxis / chemosensory behavior / intracellularly cAMP-activated cation channel activity / response to oxygen levels / thermotaxis / cation channel complex / non-motile cilium / regulation of neuron differentiation / regulation of axon extension / negative regulation of receptor guanylyl cyclase signaling pathway / monoatomic cation transmembrane transport / cGMP binding / response to hyperoxia / phototransduction / voltage-gated potassium channel activity / neuron projection morphogenesis / calcium-mediated signaling / chemotaxis / dendrite / positive regulation of gene expression / protein-containing complex binding / positive regulation of transcription by RNA polymerase II / identical protein binding / membrane / plasma membrane Similarity search - Function | ||||||||||||||||||||||||||||||||||||||||||||||||
| Biological species | ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.5 Å | ||||||||||||||||||||||||||||||||||||||||||||||||
Authors | Li, M. / Zhou, X. / Wang, S. / Michailidis, I. / Gong, Y. / Su, D. / Li, H. / Li, X. / Yang, J. | ||||||||||||||||||||||||||||||||||||||||||||||||
| Funding support | United States, China, 15items
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Citation | Journal: Nature / Year: 2017Title: Structure of a eukaryotic cyclic-nucleotide-gated channel. Authors: Minghui Li / Xiaoyuan Zhou / Shu Wang / Ioannis Michailidis / Ye Gong / Deyuan Su / Huan Li / Xueming Li / Jian Yang / ![]() Abstract: Cyclic-nucleotide-gated channels are essential for vision and olfaction. They belong to the voltage-gated ion channel superfamily but their activities are controlled by intracellular cyclic ...Cyclic-nucleotide-gated channels are essential for vision and olfaction. They belong to the voltage-gated ion channel superfamily but their activities are controlled by intracellular cyclic nucleotides instead of transmembrane voltage. Here we report a 3.5-Å-resolution single-particle electron cryo-microscopy structure of a cyclic-nucleotide-gated channel from Caenorhabditis elegans in the cyclic guanosine monophosphate (cGMP)-bound open state. The channel has an unusual voltage-sensor-like domain, accounting for its deficient voltage dependence. A carboxy-terminal linker connecting S6 and the cyclic-nucleotide-binding domain interacts directly with both the voltage-sensor-like domain and the pore domain, forming a gating ring that couples conformational changes triggered by cyclic nucleotide binding to the gate. The selectivity filter is lined by the carboxylate side chains of a functionally important glutamate and three rings of backbone carbonyls. This structure provides a new framework for understanding mechanisms of ion permeation, gating and channelopathy of cyclic-nucleotide-gated channels and cyclic nucleotide modulation of related channels. | ||||||||||||||||||||||||||||||||||||||||||||||||
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Structure visualization
| Movie |
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| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 5h3o.cif.gz | 430.2 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb5h3o.ent.gz | 346.3 KB | Display | PDB format |
| PDBx/mmJSON format | 5h3o.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 5h3o_validation.pdf.gz | 1 MB | Display | wwPDB validaton report |
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| Full document | 5h3o_full_validation.pdf.gz | 1.1 MB | Display | |
| Data in XML | 5h3o_validation.xml.gz | 63.3 KB | Display | |
| Data in CIF | 5h3o_validation.cif.gz | 94.1 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/h3/5h3o ftp://data.pdbj.org/pub/pdb/validation_reports/h3/5h3o | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 6656MC ![]() 6657C M: map data used to model this data C: citing same article ( |
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| Similar structure data |
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Links
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Assembly
| Deposited unit | ![]()
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Components
| #1: Protein | Mass: 84305.898 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Trichoplusia ni (cabbage looper) / References: UniProt: Q03611#2: Chemical | ChemComp-PCG / #3: Chemical | |
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-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
| Component | Name: Cyclic nucleotide-gated (CNG) channels / Type: COMPLEX / Entity ID: #1 / Source: RECOMBINANT | |||||||||||||||||||||||||
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| Molecular weight | Experimental value: NO | |||||||||||||||||||||||||
| Source (natural) | Organism: ![]() | |||||||||||||||||||||||||
| Source (recombinant) | Organism: Trichoplusia ni (cabbage looper) / Plasmid: pFastBac1 | |||||||||||||||||||||||||
| Buffer solution | pH: 7.4 | |||||||||||||||||||||||||
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| Specimen | Conc.: 0.6 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES / Details: This sample was homogeneous | |||||||||||||||||||||||||
| Specimen support | Grid material: COPPER / Grid mesh size: 400 divisions/in. / Grid type: Quantifoil R1.2/1.3 | |||||||||||||||||||||||||
| Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 281.15 K Details: Blotted for 4.0 seconds (double-sided, blot force 1), after waiting for 3.0 seconds the grid was immediately plunged into liquid ethane cooled by liquid-nitrogen. |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: FEI TITAN KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: SPOT SCAN |
| Electron lens | Mode: BRIGHT FIELD / Nominal magnification: 22500 X / Nominal defocus max: 2700 nm / Nominal defocus min: 1700 nm / Cs: 2.7 mm / Alignment procedure: COMA FREE |
| Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
| Image recording | Average exposure time: 8 sec. / Electron dose: 50 e/Å2 / Detector mode: SUPER-RESOLUTION / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
| Image scans | Sampling size: 5 µm / Width: 7676 / Height: 7420 / Movie frames/image: 32 / Used frames/image: 1-32 |
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Processing
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| CTF correction | Type: NONE | |||||||||||||||||||||||||||||||||||||||||||||
| Symmetry | Point symmetry: C4 (4 fold cyclic) | |||||||||||||||||||||||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3.5 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 99934 / Symmetry type: POINT |
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About Yorodumi






United States,
China, 15items
Citation
UCSF Chimera








PDBj



Trichoplusia ni (cabbage looper)


