|Entry||Database: PDB / ID: 6uw9|
|Title||Cryo-EM structure of the human TRPV3 K169A mutant in the presence of 2-APB, determined in lipid nanodisc|
|Components||Transient receptor potential cation channel subfamily V member 3|
|Keywords||MEMBRANE PROTEIN / ion channel TRPV3|
|Function / homology|
Function and homology information
negative regulation of hair cycle / positive regulation of calcium ion import / calcium channel activity / calcium ion transmembrane transport / response to heat / ion channel activity / receptor complex / integral component of plasma membrane / plasma membrane
Ankyrin repeat-containing domain / Ankyrin repeat-containing domain superfamily / Transient receptor potential channel, vanilloid 3 / Transient receptor potential cation channel subfamily V / Ankyrin repeat / Ion transport domain / Transient receptor potential channel, vanilloid 1-4
Transient receptor potential cation channel subfamily V member 3
|Biological species||Homo sapiens (human)|
|Method||ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.33 Å|
|Authors||Deng, Z. / Yuan, P.|
|Funding support|| United States, 1items |
|Citation||Journal: Nat. Struct. Mol. Biol. / Year: 2020|
Title: Gating of human TRPV3 in a lipid bilayer.
Authors: Zengqin Deng / Grigory Maksaev / Michael Rau / Zili Xie / Hongzhen Hu / James A J Fitzpatrick / Peng Yuan /
Abstract: The transient receptor potential cation channel subfamily V member 3 (TRPV3) channel plays a critical role in skin physiology, and mutations in TRPV3 result in the development of a congenital skin ...The transient receptor potential cation channel subfamily V member 3 (TRPV3) channel plays a critical role in skin physiology, and mutations in TRPV3 result in the development of a congenital skin disorder, Olmsted syndrome. Here we describe multiple cryo-electron microscopy structures of human TRPV3 reconstituted into lipid nanodiscs, representing distinct functional states during the gating cycle. The ligand-free, closed conformation reveals well-ordered lipids interacting with the channel and two physical constrictions along the ion-conduction pore involving both the extracellular selectivity filter and intracellular helix bundle crossing. Both the selectivity filter and bundle crossing expand upon activation, accompanied by substantial structural rearrangements at the cytoplasmic intersubunit interface. Transition to the inactivated state involves a secondary structure change of the pore-lining helix, which contains a π-helical segment in the closed and open conformations, but becomes entirely α-helical upon inactivation. Together with electrophysiological characterization, structures of TRPV3 in a lipid membrane environment provide unique insights into channel activation and inactivation mechanisms.
SummaryFull reportAbout validation report
|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
C: Transient receptor potential cation channel subfamily V member 3
D: Transient receptor potential cation channel subfamily V member 3
Mass: 90670.688 Da / Num. of mol.: 4 / Mutation: K169A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: TRPV3 / Production host: Pichia kudriavzevii (yeast) / References: UniProt: Q8NET8
|Experiment||Method: ELECTRON MICROSCOPY|
|EM experiment||Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction|
|Component||Name: human TRPV3 / Type: COMPLEX / Entity ID: 1 / Source: RECOMBINANT|
|Source (natural)||Organism: Homo sapiens (human)|
|Source (recombinant)||Organism: Komagataella pastoris (fungus)|
|Buffer solution||pH: 8|
|Specimen||Conc.: 1 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES|
|Vitrification||Cryogen name: ETHANE|
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Microscopy||Model: FEI TITAN KRIOS|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: OTHER|
|Electron lens||Mode: OTHER|
|Image recording||Electron dose: 62 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k)|
|CTF correction||Type: PHASE FLIPPING AND AMPLITUDE CORRECTION|
|3D reconstruction||Resolution: 4.33 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 66293 / Symmetry type: POINT|
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