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- PDB-7rhl: Cryo-EM structure of human rod Apo CNGA1/B1 channel with CLZ coil... -
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Open data
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Basic information
Entry | Database: PDB / ID: 7rhl | ||||||||||||
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Title | Cryo-EM structure of human rod Apo CNGA1/B1 channel with CLZ coiled coil | ||||||||||||
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![]() | TRANSPORT PROTEIN / ion channel | ||||||||||||
Function / homology | ![]() olfactory nerve maturation / detection of chemical stimulus involved in sensory perception of smell / photoreceptor cell outer segment organization / protein localization to organelle / detection of light stimulus involved in visual perception / ion channel modulating, G protein-coupled receptor signaling pathway / response to odorant / VxPx cargo-targeting to cilium / intracellular cyclic nucleotide activated cation channel complex / intracellularly cGMP-activated cation channel activity ...olfactory nerve maturation / detection of chemical stimulus involved in sensory perception of smell / photoreceptor cell outer segment organization / protein localization to organelle / detection of light stimulus involved in visual perception / ion channel modulating, G protein-coupled receptor signaling pathway / response to odorant / VxPx cargo-targeting to cilium / intracellular cyclic nucleotide activated cation channel complex / intracellularly cGMP-activated cation channel activity / Golgi-associated vesicle membrane / intracellularly cAMP-activated cation channel activity / photoreceptor cell maintenance / response to stimulus / retina homeostasis / ciliary membrane / photoreceptor outer segment membrane / monoatomic cation transmembrane transport / monoatomic cation transport / membrane depolarization / ligand-gated monoatomic ion channel activity / phototransduction / cGMP binding / photoreceptor outer segment / transmembrane transporter complex / cAMP binding / regulation of cytosolic calcium ion concentration / visual perception / Olfactory Signaling Pathway / Activation of the phototransduction cascade / terminal bouton / Inactivation, recovery and regulation of the phototransduction cascade / protein-containing complex binding / positive regulation of gene expression / plasma membrane Similarity search - Function | ||||||||||||
Biological species | ![]() | ||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.03 Å | ||||||||||||
![]() | Xue, J. / Han, Y. / Jiang, Y. | ||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Structural mechanisms of assembly, permeation, gating, and pharmacology of native human rod CNG channel. Authors: Jing Xue / Yan Han / Weizhong Zeng / Youxing Jiang / ![]() Abstract: Mammalian cyclic nucleotide-gated (CNG) channels are nonselective cation channels activated by cGMP or cAMP and play essential roles in the signal transduction of the visual and olfactory sensory ...Mammalian cyclic nucleotide-gated (CNG) channels are nonselective cation channels activated by cGMP or cAMP and play essential roles in the signal transduction of the visual and olfactory sensory systems. CNGA1, the principal component of the CNG channel from rod photoreceptors, can by itself form a functional homotetrameric channel and has been used as the model system in the majority of rod CNG studies. However, the native rod CNG functions as a heterotetramer consisting of three A1 and one B1 subunits and exhibits different functional properties than the CNGA1 homomer. Here we present the functional analysis of human rod CNGA1/B1 heterotetramer and its cryo-EM structures in apo, cGMP-bound, cAMP-bound, and L-cis-Diltiazem-blocked states. These structures, with resolution ranging from 2.6 to 3.3 Å, elucidate the structural mechanisms underlying the 3:1 subunit stoichiometry, the asymmetrical gating upon cGMP activation, and the unique pharmacological property of the native rod CNG channel. | ||||||||||||
History |
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Structure visualization
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Structure viewer | Molecule: ![]() ![]() |
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PDBx/mmCIF format | ![]() | 356.9 KB | Display | ![]() |
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PDB format | ![]() | 278.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 1019.7 KB | Display | ![]() |
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Full document | ![]() | 1 MB | Display | |
Data in XML | ![]() | 50.8 KB | Display | |
Data in CIF | ![]() | 78 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 24465MC ![]() 7rh9C ![]() 7rhgC ![]() 7rhhC ![]() 7rhiC ![]() 7rhjC ![]() 7rhkC 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: 64650.434 Da / Num. of mol.: 3 / Fragment: UNP residues 144-690 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #2: Protein | | Mass: 91039.305 Da / Num. of mol.: 1 / Fragment: UNP residues 454-1251 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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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: human rod Apo CNGA1/B1 channel with CLZ coiled coil / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT |
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Source (natural) | Organism: ![]() |
Source (recombinant) | Organism: ![]() |
Buffer solution | pH: 7.4 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE |
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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: ![]() |
Electron lens | Mode: BRIGHT FIELD |
Image recording | Electron dose: 1 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
Software | Name: PHENIX / Version: 1.19.2_4158: / Classification: refinement | ||||||||||||||||||||||||
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CTF correction | Type: PHASE FLIPPING ONLY | ||||||||||||||||||||||||
3D reconstruction | Resolution: 3.03 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 53732 / Symmetry type: POINT | ||||||||||||||||||||||||
Refine LS restraints |
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