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- PDB-7ji3: Cryo-EM structure of a proton-activated chloride channel -

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Basic information

Entry
Database: PDB / ID: 7ji3
TitleCryo-EM structure of a proton-activated chloride channel
ComponentsProton-activated chloride channel
KeywordsTRANSPORT PROTEIN / ion channel
Function / homologyTMEM206 protein / TMEM206 protein family / membrane => GO:0016020 / plasma membrane / Proton-activated chloride channel
Function and homology information
Biological speciesTakifugu bimaculatus (fish)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.46 Å
AuthorsDeng, Z. / Zhang, J. / Yuan, P.
CitationJournal: Sci Adv / Year: 2021
Title: Cryo-EM structure of a proton-activated chloride channel TMEM206.
Authors: Zengqin Deng / Yonghui Zhao / Jing Feng / Jingying Zhang / Haiyan Zhao / Michael J Rau / James A J Fitzpatrick / Hongzhen Hu / Peng Yuan /
Abstract: TMEM206 has been recently identified as an evolutionarily conserved chloride channel that underlies ubiquitously expressed, proton-activated, outwardly rectifying anion currents. Here, we report the ...TMEM206 has been recently identified as an evolutionarily conserved chloride channel that underlies ubiquitously expressed, proton-activated, outwardly rectifying anion currents. Here, we report the cryo-electron microscopy structure of pufferfish TMEM206, which forms a trimeric channel, with each subunit comprising two transmembrane segments and a large extracellular domain. An ample vestibule in the extracellular region is accessible laterally from the three side portals. The central pore contains multiple constrictions. A conserved lysine residue near the cytoplasmic end of the inner helix forms the presumed chloride ion selectivity filter. Unprecedentedly, the core structure and assembly closely resemble those of the epithelial sodium channel/degenerin family of sodium channels that are unrelated in amino acid sequence and conduct cations instead of anions. Together with electrophysiology, this work provides insights into ion conduction and gating for a new class of chloride channels that is architecturally distinct from previously characterized chloride channel families.
History
DepositionJul 22, 2020Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 3, 2021Provider: repository / Type: Initial release
Revision 1.1Mar 10, 2021Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.title / _citation_author.identifier_ORCID

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Structure visualization

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Assembly

Deposited unit
A: Proton-activated chloride channel
B: Proton-activated chloride channel
C: Proton-activated chloride channel


Theoretical massNumber of molelcules
Total (without water)158,7233
Polymers158,7233
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: microscopy
TypeNameSymmetry operationNumber
identity operation1_5551

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Components

#1: Protein Proton-activated chloride channel


Mass: 52907.641 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Takifugu bimaculatus (fish) / Gene: fugu_017091 / Production host: Komagataella pastoris (fungus) / References: UniProt: A0A4Z2BWB0*PLUS

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: TMEM206 / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT
Source (natural)Organism: Takifugu rubripes (torafugu)
Source (recombinant)Organism: pichia pas (fungus)
Buffer solutionpH: 8
SpecimenConc.: 1 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: OTHER
Electron lensMode: OTHER
Image recording
IDImaging-IDElectron dose (e/Å2)Film or detector model
1162GATAN K2 SUMMIT (4k x 4k)
2162GATAN K2 SUMMIT (4k x 4k)

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Processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 3.46 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 505115 / Symmetry type: POINT

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