|Entry||Database: PDB / ID: 6ot2|
|Title||Structure of the TRPV3 K169A sensitized mutant in apo form at 4.1 A resolution|
|Components||Transient receptor potential cation channel subfamily V member 3|
|Keywords||TRANSPORT PROTEIN / Ion channel / TRP channel / TRPV channel / Metal transport / Membrane transport / membrane protein|
|Function / homology|
Function and homology information
TRP channels / negative regulation of hair cycle / positive regulation of calcium ion import / calcium channel activity / calcium ion transmembrane transport / ion channel activity / response to heat / receptor complex / integral component of plasma membrane / plasma membrane
Transient receptor potential channel, vanilloid 1-4 / Ankyrin repeat / Ankyrin repeat-containing domain superfamily / Transient receptor potential channel, vanilloid 3 / Transient receptor potential cation channel subfamily V / Ankyrin repeat-containing domain / Ion transport domain / Ankyrin repeat / Ion transport protein / Ankyrin repeats (3 copies) ...Transient receptor potential channel, vanilloid 1-4 / Ankyrin repeat / Ankyrin repeat-containing domain superfamily / Transient receptor potential channel, vanilloid 3 / Transient receptor potential cation channel subfamily V / Ankyrin repeat-containing domain / Ion transport domain / Ankyrin repeat / Ion transport protein / Ankyrin repeats (3 copies) / Ankyrin repeat profile. / Ankyrin repeat region circular profile.
Transient receptor potential cation channel subfamily V member 3
|Biological species||Homo sapiens (human)|
|Method||ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.1 Å|
|Authors||Zubcevic, L. / Borschel, W.F. / Hsu, A.L. / Borgnia, M.J. / Lee, S.-Y.|
|Funding support||United States , 2件 |
|Citation||Journal: Elife / Year: 2019|
Title: Regulatory switch at the cytoplasmic interface controls TRPV channel gating.
Authors: Lejla Zubcevic / William F Borschel / Allen L Hsu / Mario J Borgnia / Seok-Yong Lee /
Abstract: Temperature-sensitive transient receptor potential vanilloid (thermoTRPV) channels are activated by ligands and heat, and are involved in various physiological processes. ThermoTRPV channels possess ...Temperature-sensitive transient receptor potential vanilloid (thermoTRPV) channels are activated by ligands and heat, and are involved in various physiological processes. ThermoTRPV channels possess a large cytoplasmic ring consisting of N-terminal ankyrin repeat domains (ARD) and C-terminal domains (CTD). The cytoplasmic inter-protomer interface is unique and consists of a CTD coiled around a β-sheet which makes contacts with the neighboring ARD. Despite much existing evidence that the cytoplasmic ring is important for thermoTRPV function, the mechanism by which this unique structure is involved in thermoTRPV gating has not been clear. Here, we present cryo-EM and electrophysiological studies which demonstrate that TRPV3 gating involves large rearrangements at the cytoplasmic inter-protomer interface and that this motion triggers coupling between cytoplasmic and transmembrane domains, priming the channel for opening. Furthermore, our studies unveil the role of this interface in the distinct biophysical and physiological properties of individual thermoTRPV subtypes.
SummaryFull reportAbout validation report
|Date||Deposition: May 2, 2019 / Release: May 22, 2019|
|Structure viewer||Molecule: |
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A: Transient receptor potential cation channel subfamily V member 3
B: Transient receptor potential cation channel subfamily V member 3
D: Transient receptor potential cation channel subfamily V member 3
C: Transient receptor potential cation channel subfamily V member 3
Mass: 84445.477 Da / Num. of mol.: 4 / Mutation: T96A, K169A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: TRPV3 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: Q8NET8
|Experiment||Method: ELECTRON MICROSCOPY|
|EM experiment||Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction|
|Component||Name: Human TRPV3 ion channel / Type: COMPLEX / Entity ID: 1 / Source: RECOMBINANT|
|Molecular weight||Value: 0.32 MDa / Experimental value: NO|
|Source (natural)||Organism: Homo sapiens (human)|
|Source (recombinant)||Organism: Spodoptera frugiperda (fall armyworm)|
|Buffer solution||pH: 8|
|Specimen||Conc.: 2.5 mg/ml / Details: Monodisperse sample / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES|
|Specimen support||Grid material: GOLD / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil, UltrAuFoil, R1.2/1.3|
|Vitrification||Cryogen name: ETHANE|
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Microscopy||Model: FEI TITAN KRIOS|
|Electron gun||Electron source: OTHER / Accelerating voltage: 300 kV / Illumination mode: OTHER|
|Electron lens||Mode: OTHER|
|Image recording||Electron dose: 40 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k)|
|Software||Name: PHENIX / Version: 1.12_2829: / Classification: refinement|
|CTF correction||Type: PHASE FLIPPING AND AMPLITUDE CORRECTION|
|Symmetry||Point symmetry: C4 (4 fold cyclic)|
|3D reconstruction||Resolution: 4.1 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 95184 / Num. of class averages: 1 / Symmetry type: POINT|
|Refine LS restraints|
Refinement-ID: ELECTRON MICROSCOPY
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