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- EMDB-75371: TASK-2 at pH 8.5 with 100 uM Bupivacaine -

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Basic information

Entry
Database: EMDB / ID: EMD-75371
TitleTASK-2 at pH 8.5 with 100 uM Bupivacaine
Map data
Sample
  • Complex: TASK-2 at pH 8.5 with 100 uM Bupivacaine
    • Protein or peptide: Potassium channel TASK2
    • Protein or peptide: Apolipoprotein A-I
  • Ligand: POTASSIUM ION
  • Ligand: Bupivacaine
  • Ligand: 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine
  • Ligand: Levobupivacaine
  • Ligand: water
KeywordsPOTASSIUM ION CHANNEL / K2P CHANNEL / TRANSPORT PROTEIN
Function / homology
Function and homology information


Phase 4 - resting membrane potential / Defective ABCA1 causes TGD / high-density lipoprotein particle receptor binding / peptidyl-methionine modification / HDL clearance / spherical high-density lipoprotein particle / negative regulation of response to cytokine stimulus / protein oxidation / vitamin transport / cholesterol import ...Phase 4 - resting membrane potential / Defective ABCA1 causes TGD / high-density lipoprotein particle receptor binding / peptidyl-methionine modification / HDL clearance / spherical high-density lipoprotein particle / negative regulation of response to cytokine stimulus / protein oxidation / vitamin transport / cholesterol import / negative regulation of heterotypic cell-cell adhesion / Scavenging by Class B Receptors / apolipoprotein A-I receptor binding / apolipoprotein receptor binding / negative regulation of cell adhesion molecule production / ABC transporters in lipid homeostasis / negative regulation of cytokine production involved in immune response / HDL assembly / high-density lipoprotein particle binding / phosphatidylcholine biosynthetic process / negative regulation of very-low-density lipoprotein particle remodeling / potassium ion export across plasma membrane / regulation of resting membrane potential / acylglycerol homeostasis / phosphatidylcholine-sterol O-acyltransferase activator activity / positive regulation of phospholipid efflux / cholesterol transport / Chylomicron remodeling / lipoprotein metabolic process / cellular response to lipoprotein particle stimulus / phospholipid homeostasis / Chylomicron assembly / potassium ion leak channel activity / high-density lipoprotein particle clearance / chylomicron / phospholipid efflux / high-density lipoprotein particle remodeling / reverse cholesterol transport / very-low-density lipoprotein particle / positive regulation of cholesterol metabolic process / high-density lipoprotein particle assembly / low-density lipoprotein particle / high-density lipoprotein particle / chemorepellent activity / cholesterol transfer activity / outward rectifier potassium channel activity / regulation of Cdc42 protein signal transduction / cholesterol efflux / HDL remodeling / triglyceride homeostasis / negative chemotaxis / Scavenging by Class A Receptors / negative regulation of interleukin-1 beta production / amyloid-beta formation / positive regulation of Rho protein signal transduction / potassium ion import across plasma membrane / cholesterol binding / cholesterol metabolic process / positive regulation of cholesterol efflux / positive regulation of substrate adhesion-dependent cell spreading / potassium channel activity / positive regulation of stress fiber assembly / negative regulation of tumor necrosis factor-mediated signaling pathway / Scavenging of heme from plasma / endocytic vesicle / voltage-gated potassium channel activity / Retinoid metabolism and transport / Dengue virus activates/modulates innate and adaptive immune responses / heat shock protein binding / endocytic vesicle lumen / cholesterol homeostasis / positive regulation of phagocytosis / integrin-mediated signaling pathway / potassium ion transmembrane transport / Post-translational protein phosphorylation / Heme signaling / Maturation of DENV proteins / PPARA activates gene expression / negative regulation of inflammatory response / phospholipid binding / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / Platelet degranulation / amyloid-beta binding / extracellular vesicle / Dengue Virus-Host Interactions / secretory granule lumen / cytoplasmic vesicle / blood microparticle / early endosome / protein stabilization / G protein-coupled receptor signaling pathway / protein heterodimerization activity / receptor ligand activity / endoplasmic reticulum lumen / Amyloid fiber formation / signaling receptor binding / enzyme binding / protein homodimerization activity / extracellular exosome / extracellular region
Similarity search - Function
Two pore domain potassium channel, TASK family / Apolipoprotein A/E / : / Apolipoprotein A1/A4/E domain / Two pore domain potassium channel / Potassium channel domain / Ion channel
Similarity search - Domain/homology
Apolipoprotein A-I / Potassium channel TASK2
Similarity search - Component
Biological speciesMus musculus (house mouse) / Homo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.06 Å
AuthorsDocter T / Li B / 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: To Be Published
Title: A shared site for lipid and anesthetic block of the two-pore domain K+ channel TASK-2
Authors: Docter T / Sorum B / Li B / Rietmeijer RA / Cook ASI / Kotecha A / Brohawn SG
History
DepositionJan 30, 2026-
Header (metadata) releaseOct 7, 2026-
Map releaseOct 7, 2026-
UpdateOct 7, 2026-
Current statusOct 7, 2026Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

Downloads & links

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Map

FileDownload / File: emd_75371.map.gz / Format: CCP4 / Size: 125 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.57 Å/pix.
x 320 pix.
= 182.4 Å
0.57 Å/pix.
x 320 pix.
= 182.4 Å
0.57 Å/pix.
x 320 pix.
= 182.4 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.57 Å
Density
Contour LevelBy AUTHOR: 0.226
Minimum - Maximum-1.2371151 - 1.7771548
Average (Standard dev.)0.002459511 (±0.0443021)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions320320320
Spacing320320320
CellA=B=C: 182.4 Å
α=β=γ: 90.0 °

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Supplemental data

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Additional map: #1

Fileemd_75371_additional_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Half map: #2

Fileemd_75371_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Half map: #1

Fileemd_75371_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Sample components

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Entire : TASK-2 at pH 8.5 with 100 uM Bupivacaine

EntireName: TASK-2 at pH 8.5 with 100 uM Bupivacaine
Components
  • Complex: TASK-2 at pH 8.5 with 100 uM Bupivacaine
    • Protein or peptide: Potassium channel TASK2
    • Protein or peptide: Apolipoprotein A-I
  • Ligand: POTASSIUM ION
  • Ligand: Bupivacaine
  • Ligand: 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine
  • Ligand: Levobupivacaine
  • Ligand: water

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Supramolecule #1: TASK-2 at pH 8.5 with 100 uM Bupivacaine

SupramoleculeName: TASK-2 at pH 8.5 with 100 uM Bupivacaine / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 77 KDa

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Macromolecule #1: Potassium channel TASK2

MacromoleculeName: Potassium channel TASK2 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 38.661832 KDa
Recombinant expressionOrganism: Komagataella pastoris (fungus)
SequenceString: MVDRGPLLTS AIIFYLAIGA AIFEVLEEPH WKEAKKNYYT QKLHLLKEFP CLSQEGLDKI LQVVSDAADQ GVAITGNQTF NNWNWPNAM IFAATVITTI GYGNVAPKTP AGRLFCVFYG LFGVPLCLTW ISALGKFFGG RAKRLGQFLT RRGVSLRKAQ I TCTAIFIV ...String:
MVDRGPLLTS AIIFYLAIGA AIFEVLEEPH WKEAKKNYYT QKLHLLKEFP CLSQEGLDKI LQVVSDAADQ GVAITGNQTF NNWNWPNAM IFAATVITTI GYGNVAPKTP AGRLFCVFYG LFGVPLCLTW ISALGKFFGG RAKRLGQFLT RRGVSLRKAQ I TCTAIFIV WGVLVHLVIP PFVFMVTEEW NYIEGLYYSF ITISTIGFGD FVAGVNPSAN YHALYRYFVE LWIYLGLAWL SL FVNWKVS MFVEVHKAIK KRRRRRKESF ESSPHSRKAL QMAGSTASKD VNIFSFLSKK EETYNDLIKQ IGKKAMKTSG GGE RVPGPG HGLGPQGDRS NSLEVLFQ

UniProtKB: Potassium channel TASK2

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Macromolecule #2: Apolipoprotein A-I

MacromoleculeName: Apolipoprotein A-I / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 24.704729 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: GHHHHHHHDY DIPTTENLYF QGSTFSKLRE QLGPVTQEFW DNLEKETEGL RQEMSKDLEE VKAKVQPYLD DFQKKWQEEM ELYRQKVEP LRAELQEGAR QKLHELQEKL SPLGEEMRDR ARAHVDALRT HLAPYSDELR QRLAARLEAL KENGGARLAE Y HAKATEHL ...String:
GHHHHHHHDY DIPTTENLYF QGSTFSKLRE QLGPVTQEFW DNLEKETEGL RQEMSKDLEE VKAKVQPYLD DFQKKWQEEM ELYRQKVEP LRAELQEGAR QKLHELQEKL SPLGEEMRDR ARAHVDALRT HLAPYSDELR QRLAARLEAL KENGGARLAE Y HAKATEHL STLSEKAKPA LEDLRQGLLP VLESFKVSFL SALEEYTKKL NTQ

UniProtKB: Apolipoprotein A-I

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Macromolecule #3: POTASSIUM ION

MacromoleculeName: POTASSIUM ION / type: ligand / ID: 3 / Number of copies: 4 / Formula: K
Molecular weightTheoretical: 39.098 Da

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Macromolecule #4: Bupivacaine

MacromoleculeName: Bupivacaine / type: ligand / ID: 4 / Number of copies: 1 / Formula: A1C7A
Molecular weightTheoretical: 288.428 Da

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Macromolecule #5: 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine

MacromoleculeName: 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine / type: ligand / ID: 5 / Number of copies: 14 / Formula: PEE
Molecular weightTheoretical: 744.034 Da
Chemical component information

ChemComp-PEE:
1,2-dioleoyl-sn-glycero-3-phosphoethanolamine / DOPE, phospholipid*YM

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Macromolecule #6: Levobupivacaine

MacromoleculeName: Levobupivacaine / type: ligand / ID: 6 / Number of copies: 1 / Formula: OJ0
Molecular weightTheoretical: 288.428 Da
Chemical component information

ChemComp-OJ0:
Levobupivacaine

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Macromolecule #7: water

MacromoleculeName: water / type: ligand / ID: 7 / Number of copies: 21 / Formula: HOH
Molecular weightTheoretical: 18.015 Da
Chemical component information

ChemComp-HOH:
WATER

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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

BufferpH: 8.5
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: TFS FALCON 4i (4k 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: 1.5 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:
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.06 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 29149
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

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