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- PDB-6wel: Structure of cGMP-unbound F403V/V407A mutant TAX-4 reconstituted ... -
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Basic information
Entry | Database: PDB / ID: 6wel | |||||||||||||||||||||
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Title | Structure of cGMP-unbound F403V/V407A mutant TAX-4 reconstituted in lipid nanodiscs | |||||||||||||||||||||
![]() | Cyclic nucleotide-gated cation channel | |||||||||||||||||||||
![]() | MEMBRANE PROTEIN / Ion channel / vision / olfaction / phototransduction / blindness / cyclic nucleotide-gated channel / lipid nanodiscs | |||||||||||||||||||||
Function / homology | ![]() detection of carbon dioxide / detection of chemical stimulus involved in sensory perception / ciliary inversin compartment / Activation of the phototransduction cascade / Inactivation, recovery and regulation of the phototransduction cascade / VxPx cargo-targeting to cilium / thermosensory behavior / positive regulation of growth rate / olfactory behavior / aerotaxis ...detection of carbon dioxide / detection of chemical stimulus involved in sensory perception / ciliary inversin compartment / Activation of the phototransduction cascade / Inactivation, recovery and regulation of the phototransduction cascade / VxPx cargo-targeting to cilium / thermosensory behavior / positive regulation of growth rate / olfactory behavior / aerotaxis / chemosensory behavior / intracellular cyclic nucleotide activated cation channel complex / G protein-coupled receptor signaling pathway coupled to cGMP nucleotide second messenger / multicellular organismal reproductive process / intracellularly cGMP-activated cation channel activity / cation channel complex / response to oxygen levels / intracellularly cAMP-activated cation channel activity / thermotaxis / non-motile cilium / regulation of neuron differentiation / regulation of axon extension / negative regulation of cGMP-mediated signaling / voltage-gated potassium channel activity / monoatomic cation transmembrane transport / phototransduction / cGMP binding / response to hyperoxia / 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: 2.5 Å | |||||||||||||||||||||
![]() | Zheng, X. / Fu, Z. / Su, D. / Zhang, Y. / Li, M. / Pan, Y. / Li, H. / Li, S. / Grassucci, R.A. / Ren, Z. ...Zheng, X. / Fu, Z. / Su, D. / Zhang, Y. / Li, M. / Pan, Y. / Li, H. / Li, S. / Grassucci, R.A. / Ren, Z. / Hu, Z. / Li, X. / Zhou, M. / Li, G. / Frank, J. / Yang, J. | |||||||||||||||||||||
Funding support | ![]() ![]()
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![]() | ![]() Title: Mechanism of ligand activation of a eukaryotic cyclic nucleotide-gated channel. Authors: Xiangdong Zheng / Ziao Fu / Deyuan Su / Yuebin Zhang / Minghui Li / Yaping Pan / Huan Li / Shufang Li / Robert A Grassucci / Zhenning Ren / Zhengshan Hu / Xueming Li / Ming Zhou / Guohui Li ...Authors: Xiangdong Zheng / Ziao Fu / Deyuan Su / Yuebin Zhang / Minghui Li / Yaping Pan / Huan Li / Shufang Li / Robert A Grassucci / Zhenning Ren / Zhengshan Hu / Xueming Li / Ming Zhou / Guohui Li / Joachim Frank / Jian Yang / ![]() ![]() Abstract: Cyclic nucleotide-gated (CNG) channels convert cyclic nucleotide (CN) binding and unbinding into electrical signals in sensory receptors and neurons. The molecular conformational changes underpinning ...Cyclic nucleotide-gated (CNG) channels convert cyclic nucleotide (CN) binding and unbinding into electrical signals in sensory receptors and neurons. The molecular conformational changes underpinning ligand activation are largely undefined. We report both closed- and open-state atomic cryo-EM structures of a full-length Caenorhabditis elegans cyclic GMP-activated channel TAX-4, reconstituted in lipid nanodiscs. These structures, together with computational and functional analyses and a mutant channel structure, reveal a double-barrier hydrophobic gate formed by two S6 amino acids in the central cavity. cGMP binding produces global conformational changes that open the cavity gate located ~52 Å away but do not alter the structure of the selectivity filter-the commonly presumed activation gate. Our work provides mechanistic insights into the allosteric gating and regulation of CN-gated and nucleotide-modulated channels and CNG channel-related channelopathies. | |||||||||||||||||||||
History |
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Structure visualization
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Structure viewer | Molecule: ![]() ![]() |
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PDBx/mmCIF format | ![]() | 399.8 KB | Display | ![]() |
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PDB format | ![]() | 333.9 KB | Display | ![]() |
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-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 21651MC ![]() 6wejC ![]() 6wekC C: citing same article ( M: map data used to model this data |
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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: 83914.523 Da / Num. of mol.: 4 / Mutation: F403V, V407A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Chemical | ChemComp-CPL / #3: Chemical | ChemComp-PX2 / #4: Chemical | ChemComp-NA / | 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 |
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Sample preparation
Component | Name: Structure of cGMP-unbound F403V/V407A mutant TAX-4 reconstituted in lipid nanodiscs Type: COMPLEX / Entity ID: #1 / 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 | Cryogen name: ETHANE-PROPANE |
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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: OTHER |
Image recording | Electron dose: 56.45 e/Å2 / Detector mode: COUNTING / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
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Processing
EM software |
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CTF correction | Type: NONE | |||||||||||||||||||||||||||||||||
Particle selection | Num. of particles selected: 1877870 | |||||||||||||||||||||||||||||||||
Symmetry | Point symmetry: C4 (4 fold cyclic) | |||||||||||||||||||||||||||||||||
3D reconstruction | Resolution: 2.5 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 445131 / Symmetry type: POINT | |||||||||||||||||||||||||||||||||
Atomic model building | Protocol: RIGID BODY FIT | |||||||||||||||||||||||||||||||||
Atomic model building | PDB-ID: 5H3O |