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- EMDB-21651: Structure of cGMP-unbound F403V/V407A mutant TAX-4 reconstituted ... -
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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-21651 | |||||||||||||||||||||
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Title | Structure of cGMP-unbound F403V/V407A mutant TAX-4 reconstituted in lipid nanodiscs | |||||||||||||||||||||
![]() | cGMP-unbound F403V/V407A mutant TAX-4 reconstituted in lipid nanodiscs | |||||||||||||||||||||
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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 | 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 RA / Ren Z ...Zheng X / Fu Z / Su D / Zhang Y / Li M / Pan Y / Li H / Li S / Grassucci RA / 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 | EM map: ![]() ![]() ![]() |
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 93.3 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 15.5 KB 15.5 KB | Display Display | ![]() |
Images | ![]() | 71.9 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6welMC ![]() 6wejC ![]() 6wekC C: citing same article ( M: atomic model generated by this map |
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Similar structure data |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Annotation | cGMP-unbound F403V/V407A mutant TAX-4 reconstituted in lipid nanodiscs | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.06 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
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Sample components
-Entire : Structure of cGMP-unbound F403V/V407A mutant TAX-4 reconstituted ...
Entire | Name: Structure of cGMP-unbound F403V/V407A mutant TAX-4 reconstituted in lipid nanodiscs |
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Components |
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-Supramolecule #1: Structure of cGMP-unbound F403V/V407A mutant TAX-4 reconstituted ...
Supramolecule | Name: Structure of cGMP-unbound F403V/V407A mutant TAX-4 reconstituted in lipid nanodiscs type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 |
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Source (natural) | Organism: ![]() ![]() |
Recombinant expression | Organism: ![]() ![]() |
-Macromolecule #1: Cyclic nucleotide-gated cation channel
Macromolecule | Name: Cyclic nucleotide-gated cation channel / type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 83.914523 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MSTAEPAPDP TNPSTSGLAP TTNGIGSPPP TASAATKFSI LTKFLRRKNQ VHTTTAQQNE FMQKYMPNGN SNAVQPAATG GQPASSDGG SAIEVPPPKE SYAVRIRKYL ANYTQDPSTD NFYYWTCVVT VAYIYNLLFV IARQVFNDLI GPSSQSLCRF Y NGTLNSTT ...String: MSTAEPAPDP TNPSTSGLAP TTNGIGSPPP TASAATKFSI LTKFLRRKNQ VHTTTAQQNE FMQKYMPNGN SNAVQPAATG GQPASSDGG SAIEVPPPKE SYAVRIRKYL ANYTQDPSTD NFYYWTCVVT VAYIYNLLFV IARQVFNDLI GPSSQSLCRF Y NGTLNSTT QVECTYNMLT NMKEMPTYSQ YPDLGWSKYW HFRMLWVFFD LLMDCVYLID TFLNYRMGYM DQGLVVREAE KV TKAYWQS KQYRIDGISL IPLDYILGWP IPYINWRGLP ILRLNRLIRY KRVRNCLERT ETRSSMPNAF RVVVVVWYIV III HWNACL YFWISEWIGL GTDAWVYGHL NKQSLPDDIT DTLLRRYVYS FYWSTLILTT IGEVPSPVRN IEYAFVTLDL MCGV LIVAT IAGNVGSMIS NMSAARTEFQ NKMDGIKQYM ELRKVSKQLE IRVIKWFDYL WTNKQSLSDQ QVLKVLPDKL QAEIA MQVH FETLRKVRIF QDCEAGLLAE LVLKLQLQVF SPGDFICKKG DIGREMYIVK RGRLQVVDDD GKKVFVTLQE GSVFGE LSI LNIAGSKNGN RRTANVRSVG YTDLFVLSKT DLWNALREYP DARKLLLAKG REILKKDNLL DENAPEEQKT VEEIAEH LN NAVKVLQTRM ARLIVEHSST EGKLMKRIEM LEKHLSRYKA LARRQKTMHG VSIDGGDIST DGVDERVRPP RLRQTKTI D LPTGTESESL LK |
-Macromolecule #2: 1-PALMITOYL-2-LINOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE
Macromolecule | Name: 1-PALMITOYL-2-LINOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE / type: ligand / ID: 2 / Number of copies: 28 / Formula: CPL |
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Molecular weight | Theoretical: 758.06 Da |
Chemical component information | ![]() ChemComp-CPL: |
-Macromolecule #3: 1,2-DILAUROYL-SN-GLYCERO-3-PHOSPHATE
Macromolecule | Name: 1,2-DILAUROYL-SN-GLYCERO-3-PHOSPHATE / type: ligand / ID: 3 / Number of copies: 8 / Formula: PX2 |
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Molecular weight | Theoretical: 535.671 Da |
Chemical component information | ![]() ChemComp-PX2: |
-Macromolecule #4: SODIUM ION
Macromolecule | Name: SODIUM ION / type: ligand / ID: 4 / Number of copies: 1 |
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Molecular weight | Theoretical: 22.99 Da |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.4 |
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Vitrification | Cryogen name: ETHANE-PROPANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: COUNTING / Average electron dose: 56.45 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: OTHER |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |