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Yorodumi- PDB-7o4h: The structure of the native CNGA1/CNGB1 CNG channel from retinal rods -
+Open data
-Basic information
Entry | Database: PDB / ID: 7o4h | ||||||
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Title | The structure of the native CNGA1/CNGB1 CNG channel from retinal rods | ||||||
Components |
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Keywords | MEMBRANE PROTEIN / CNG channel / CNGA1 / CNGB1 / rod | ||||||
Function / homology | Function and homology information non-motile cilium membrane / intracellular cyclic nucleotide activated cation channel complex / intracellularly cGMP-activated cation channel activity / rod photoreceptor outer segment / intracellularly cAMP-activated cation channel activity / Inactivation, recovery and regulation of the phototransduction cascade / Activation of the phototransduction cascade / molecular sequestering activity / retina homeostasis / sodium channel activity ...non-motile cilium membrane / intracellular cyclic nucleotide activated cation channel complex / intracellularly cGMP-activated cation channel activity / rod photoreceptor outer segment / intracellularly cAMP-activated cation channel activity / Inactivation, recovery and regulation of the phototransduction cascade / Activation of the phototransduction cascade / molecular sequestering activity / retina homeostasis / sodium channel activity / photoreceptor outer segment membrane / sodium ion transport / monoatomic cation transmembrane transport / monoatomic cation transport / cGMP binding / photoreceptor outer segment / transmembrane transporter complex / cAMP binding / visual perception / calcium channel activity / potassium ion transport / sensory perception of smell / calcium ion transport / molecular adaptor activity / protein-containing complex binding / positive regulation of gene expression / protein homodimerization activity / protein-containing complex / identical protein binding / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | Bos taurus (cattle) | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.4 Å | ||||||
Authors | Barret, D.C.A. / Marino, J. | ||||||
Funding support | Switzerland, 1items
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Citation | Journal: Nat Struct Mol Biol / Year: 2022 Title: The structure of the native CNGA1/CNGB1 CNG channel from bovine retinal rods. Authors: Diane C A Barret / Gebhard F X Schertler / U Benjamin Kaupp / Jacopo Marino / Abstract: In rod photoreceptors of the retina, the cyclic nucleotide-gated (CNG) channel is composed of three CNGA and one CNGB subunits, and it closes in response to light activation to generate an electrical ...In rod photoreceptors of the retina, the cyclic nucleotide-gated (CNG) channel is composed of three CNGA and one CNGB subunits, and it closes in response to light activation to generate an electrical signal that is conveyed to the brain. Here we report the cryo-EM structure of the closed state of the native rod CNG channel isolated from bovine retina. The structure reveals differences between CNGA1 and CNGB1 subunits. Three CNGA1 subunits are tethered at their C terminus by a coiled-coil region. The C-helix in the cyclic nucleotide-binding domain of CNGB1 features a different orientation from that in the three CNGA1 subunits. The arginine residue R994 of CNGB1 reaches into the ionic pathway and blocks the pore, thus introducing an additional gate, which is different from the central hydrophobic gate known from homomeric CNGA channels. These results address the long-standing question of how CNGB1 subunits contribute to the function of CNG channels in visual and olfactory neurons. | ||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | Molecule: MolmilJmol/JSmol |
-Downloads & links
-Download
PDBx/mmCIF format | 7o4h.cif.gz | 346.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb7o4h.ent.gz | 265.6 KB | Display | PDB format |
PDBx/mmJSON format | 7o4h.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 7o4h_validation.pdf.gz | 895.2 KB | Display | wwPDB validaton report |
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Full document | 7o4h_full_validation.pdf.gz | 929.7 KB | Display | |
Data in XML | 7o4h_validation.xml.gz | 53.6 KB | Display | |
Data in CIF | 7o4h_validation.cif.gz | 79.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/o4/7o4h ftp://data.pdbj.org/pub/pdb/validation_reports/o4/7o4h | HTTPS FTP |
-Related structure data
Related structure data | 12718MC M: map data used to model this data C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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-Components
#1: Protein | Mass: 79712.164 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / References: UniProt: Q00194 #2: Protein | | Mass: 155228.562 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / References: UniProt: Q28181 Has ligand of interest | N | |
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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 |
-Sample preparation
Component | Name: Native CNGA1/CNGB1a channel / Type: COMPLEX / Details: purified from rod outer segments / Entity ID: all / Source: NATURAL |
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Molecular weight | Value: 0.356 MDa / Experimental value: NO |
Source (natural) | Organism: Bos taurus (cattle) |
Buffer solution | pH: 7.5 |
Specimen | Conc.: 0.3 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE |
-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: FLOOD BEAM |
Electron lens | Mode: BRIGHT FIELD |
Image recording | Electron dose: 1.5 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
-Processing
Software | Name: PHENIX / Version: 1.18.2_3874: / Classification: refinement | ||||||||||||||||||||||||
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EM software |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
3D reconstruction | Resolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 118084 / Symmetry type: POINT | ||||||||||||||||||||||||
Refine LS restraints |
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