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- EMDB-48632: Mus musculus TASK-1 (KCNK3) in MSP1E3D1 lipid nanodisc at pH 6.0 ... -

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Basic information

Entry
Database: EMDB / ID: EMD-48632
TitleMus musculus TASK-1 (KCNK3) in MSP1E3D1 lipid nanodisc at pH 6.0 and 100 mM KCl
Map dataSharpened map
Sample
  • Complex: TASK-1 in MSP1E3D1 lipid nanodisc
    • Protein or peptide: Potassium channel subfamily K member 3
  • Ligand: POTASSIUM ION
  • Ligand: CHOLESTEROL HEMISUCCINATE
KeywordsK2P / MEMBRANE PROTEIN / POTASSIUM CHANNEL / ION CHANNEL
Function / homology
Function and homology information


TWIK-releated acid-sensitive K+ channel (TASK) / detection of hypoxic conditions in blood by carotid body chemoreceptor signaling / open rectifier potassium channel activity / positive regulation of voltage-gated potassium channel activity / Phase 4 - resting membrane potential / regulation of action potential firing rate / potassium ion leak channel activity / regulation of resting membrane potential / S100 protein binding / outward rectifier potassium channel activity ...TWIK-releated acid-sensitive K+ channel (TASK) / detection of hypoxic conditions in blood by carotid body chemoreceptor signaling / open rectifier potassium channel activity / positive regulation of voltage-gated potassium channel activity / Phase 4 - resting membrane potential / regulation of action potential firing rate / potassium ion leak channel activity / regulation of resting membrane potential / S100 protein binding / outward rectifier potassium channel activity / cellular response to zinc ion / negative regulation of cytosolic calcium ion concentration / sodium channel activity / cochlea development / monoatomic ion channel activity / potassium ion transport / cellular response to acidic pH / potassium ion transmembrane transport / cellular response to hypoxia / monoatomic ion transmembrane transport / response to xenobiotic stimulus / protein heterodimerization activity / plasma membrane
Similarity search - Function
Potassium channel subfamily K member 3 / Two pore domain potassium channel, TASK family / Two pore domain potassium channel / Potassium channel domain / Ion channel
Similarity search - Domain/homology
Potassium channel subfamily K member 3
Similarity search - Component
Biological speciesMus musculus (house mouse)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.1 Å
AuthorsDocter TA / Brohawn SG
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM145869 United States
CitationJournal: Structure / Year: 2026
Title: Structural basis for proton inhibition of the two-pore domain K channel TASK-1.
Authors: Trevor Docter / Nicolas S Lee / Michelle S Reid / Stephen G Brohawn /
Abstract: TASK-1 is a pH-sensitive two-pore domain K channel implicated in diseases including pulmonary arterial hypertension (PAH) and developmental delay with sleep apnea (DDSA). Structures of TASK-1 have ...TASK-1 is a pH-sensitive two-pore domain K channel implicated in diseases including pulmonary arterial hypertension (PAH) and developmental delay with sleep apnea (DDSA). Structures of TASK-1 have been captured with an open external gate, but the structural basis for external proton inhibition is incompletely understood. Here, we present a cryo-EM structure of TASK-1 at pH 6.0 and 100 mM K, revealing a closed extracellular gate. pH-regulation of TASK-1 involves a C-type selectivity filter gate similar to TASK-3, but distinct from other K2Ps, in which histidine protonation leads to the formation of a hydrophobic seal above the filter. We find that a PAH-associated loss-of-function mutation near the outer gate increases proton sensitivity, while DDSA-associated and other gain-of-function mutations near the inner X-gate and cavity reduce proton sensitivity. These data reveal the mechanism for pH regulation of TASK-1, illustrate differences in C-type gating among K2Ps, and suggest allosteric communication between inner and outer gates.
History
DepositionJan 13, 2025-
Header (metadata) releaseJan 28, 2026-
Map releaseJan 28, 2026-
UpdateJul 15, 2026-
Current statusJul 15, 2026Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_48632.png

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Map

FileDownload / File: emd_48632.map.gz / Format: CCP4 / Size: 91.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationSharpened map
Projections & slices

Image control

Size
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AxesZ (Sec.)Y (Row.)X (Col.)
1.05 Å/pix.
x 288 pix.
= 301.824 Å		1.05 Å/pix.
x 288 pix.
= 301.824 Å		1.05 Å/pix.
x 288 pix.
= 301.824 Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.048 Å
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Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.3
Minimum - Maximum-1.2396518 - 2.0089483
Average (Standard dev.)0.00046364332 (±0.027433427)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions288288288
Spacing288288288
CellA=B=C: 301.824 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_48632_msk_1.map
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Additional map: Unsharpened map

Fileemd_48632_additional_1.map
AnnotationUnsharpened map
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Additional map: C2 symmetric map

Fileemd_48632_additional_2.map
AnnotationC2 symmetric map
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Half map: Half map A

Fileemd_48632_half_map_1.map
AnnotationHalf map A
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Half map: Half map B

Fileemd_48632_half_map_2.map
AnnotationHalf map B
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Sample components

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Entire : TASK-1 in MSP1E3D1 lipid nanodisc

EntireName: TASK-1 in MSP1E3D1 lipid nanodisc
Components
  • Complex: TASK-1 in MSP1E3D1 lipid nanodisc
    • Protein or peptide: Potassium channel subfamily K member 3
  • Ligand: POTASSIUM ION
  • Ligand: CHOLESTEROL HEMISUCCINATE

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Supramolecule #1: TASK-1 in MSP1E3D1 lipid nanodisc

SupramoleculeName: TASK-1 in MSP1E3D1 lipid nanodisc / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 60 KDa

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Macromolecule #1: Potassium channel subfamily K member 3

MacromoleculeName: Potassium channel subfamily K member 3 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 30.211213 KDa
Recombinant expressionOrganism: Komagataella pastoris (fungus)
SequenceString: MKRQNVRTLA LIVCTFTYLL VGAAVFDALE SEPEMIERQR LELRQLELRA RYNLSEGGYE ELERVVLRLK PHKAGVQWRF AGSFYFAIT VITTIGYGHA APSTDGGKVF CMFYALLGIP LTLVMFQSLG ERINTFVRYL LHRAKRGLGM RHAEVSMANM V LIGFVSCI ...String:
MKRQNVRTLA LIVCTFTYLL VGAAVFDALE SEPEMIERQR LELRQLELRA RYNLSEGGYE ELERVVLRLK PHKAGVQWRF AGSFYFAIT VITTIGYGHA APSTDGGKVF CMFYALLGIP LTLVMFQSLG ERINTFVRYL LHRAKRGLGM RHAEVSMANM V LIGFVSCI STLCIGAAAF SYYERWTFFQ AYYYCFITLT TIGFGDYVAL QKDQALQTQP QYVAFSFVYI LTGLTVIGAF LN LVVLRFM TMNAEDEKRS NSLEVLFQ

UniProtKB: Potassium channel subfamily K member 3

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Macromolecule #2: POTASSIUM ION

MacromoleculeName: POTASSIUM ION / type: ligand / ID: 2 / Number of copies: 2 / Formula: K
Molecular weightTheoretical: 39.098 Da

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Macromolecule #3: CHOLESTEROL HEMISUCCINATE

MacromoleculeName: CHOLESTEROL HEMISUCCINATE / type: ligand / ID: 3 / Number of copies: 2 / Formula: Y01
Molecular weightTheoretical: 486.726 Da
Chemical component information

ChemComp-Y01:
CHOLESTEROL HEMISUCCINATE

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

Concentration0.5 mg/mL
BufferpH: 6
Component:
ConcentrationFormulaName
20.0 mMC6H13NO4SMES
100.0 mMKClPotassium chloride
1.0 mMC10H16N2O8EDTA
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.8 µm / Nominal defocus min: 0.5 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: PDB ENTRY
PDB model - PDB ID:

6rv2

Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 3.1 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 106442
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

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