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Yorodumi- PDB-7lfw: Cryo-EM structure of human cGMP-bound open CNGA1 channel in K+/Ca2+ -
+Open data
-Basic information
Entry | Database: PDB / ID: 7lfw | |||||||||
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Title | Cryo-EM structure of human cGMP-bound open CNGA1 channel in K+/Ca2+ | |||||||||
Components | cGMP-gated cation channel alpha-1 | |||||||||
Keywords | MEMBRANE PROTEIN / ALPHA-HELICAL / ION CHANNEL | |||||||||
Function / homology | Function and homology information intracellular cyclic nucleotide activated cation channel complex / intracellularly cGMP-activated cation channel activity / rod photoreceptor outer segment / intracellularly cAMP-activated cation channel activity / sodium channel activity / photoreceptor outer segment membrane / sodium ion transport / monoatomic cation transmembrane transport / cGMP binding / cAMP binding ...intracellular cyclic nucleotide activated cation channel complex / intracellularly cGMP-activated cation channel activity / rod photoreceptor outer segment / intracellularly cAMP-activated cation channel activity / sodium channel activity / photoreceptor outer segment membrane / sodium ion transport / monoatomic cation transmembrane transport / cGMP binding / cAMP binding / visual perception / calcium channel activity / Activation of the phototransduction cascade / calcium ion transport / Inactivation, recovery and regulation of the phototransduction cascade / protein-containing complex binding / plasma membrane Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.9 Å | |||||||||
Authors | Xue, J. / Han, Y. / Jiang, Y. | |||||||||
Funding support | United States, 2items
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Citation | Journal: Neuron / Year: 2021 Title: Structural mechanisms of gating and selectivity of human rod CNGA1 channel. Authors: Jing Xue / Yan Han / Weizhong Zeng / Yan Wang / Youxing Jiang / Abstract: Mammalian cyclic nucleotide-gated (CNG) channels play an essential role in the signal transduction of the visual and olfactory sensory systems. Here we reveal the structural mechanism of ligand ...Mammalian cyclic nucleotide-gated (CNG) channels play an essential role in the signal transduction of the visual and olfactory sensory systems. Here we reveal the structural mechanism of ligand gating in human rod CNGA1 channel by determining its cryo-EM structures in both the apo closed and cGMP-bound open states. Distinct from most other members of voltage-gated tetrameric cation channels, CNGA1 forms a central channel gate in the middle of the membrane, occluding the central cavity. Structural analyses of ion binding profiles in the selectivity filters of the wild-type channel and the E365Q filter mutant allow us to unambiguously define the two Ca binding sites inside the selectivity filter, providing structural insights into Ca blockage and permeation in CNG channels. The structure of the E365Q mutant also reveals two alternative side-chain conformations at Q365, providing a plausible explanation for the voltage-dependent gating of CNG channel acquired upon E365 mutation. | |||||||||
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 | 7lfw.cif.gz | 328.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb7lfw.ent.gz | 266.5 KB | Display | PDB format |
PDBx/mmJSON format | 7lfw.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 7lfw_validation.pdf.gz | 1.2 MB | Display | wwPDB validaton report |
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Full document | 7lfw_full_validation.pdf.gz | 1.3 MB | Display | |
Data in XML | 7lfw_validation.xml.gz | 58.7 KB | Display | |
Data in CIF | 7lfw_validation.cif.gz | 85.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lf/7lfw ftp://data.pdbj.org/pub/pdb/validation_reports/lf/7lfw | HTTPS FTP |
-Related structure data
Related structure data | 23307MC 7lftC 7lfxC 7lfyC 7lg1C 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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1 |
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-Components
#1: Protein | Mass: 64650.434 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: CNGA1, CNCG, CNCG1 / Production host: Homo sapiens (human) / References: UniProt: P29973 #2: Chemical | ChemComp-PCG / #3: Chemical | Has ligand of interest | Y | |
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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: cGMP-bound open CNGA1 homotetramer in K+/Ca2+ / Type: CELL / Entity ID: #1 / Source: MULTIPLE SOURCES |
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Source (natural) | Organism: Homo sapiens (human) |
Source (recombinant) | Organism: Homo sapiens (human) |
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 |
-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 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
-Processing
CTF correction | Type: PHASE FLIPPING ONLY |
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3D reconstruction | Resolution: 2.9 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 322961 / Symmetry type: POINT |