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- PDB-10pb: TASK-2 L127N at pH 6.5 -

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Basic information

Entry
Database: PDB / ID: 10pb
TitleTASK-2 L127N at pH 6.5
Components
  • Apolipoprotein A-I
  • Potassium channel TASK2
KeywordsTRANSPORT PROTEIN / POTASSIUM ION CHANNEL / K2P CHANNEL
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
: / 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine / Apolipoprotein A-I / Potassium channel TASK2
Similarity search - Component
Biological speciesMus musculus (house mouse)
Homo sapiens (human)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.75 Å
AuthorsDocter, T. / Li, B. / Brohawn, S.G.
Funding support United States, 1items
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, R.A. / Cook, A.S.I. / Kotecha, A. / Brohawn, S.G.
History
DepositionJan 30, 2026Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 7, 2026Provider: repository / Type: Initial release
Revision 1.0Oct 7, 2026Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Potassium channel TASK2
B: Potassium channel TASK2
D: Apolipoprotein A-I
hetero molecules


Theoretical massNumber of molelcules
Total (without water)117,02826
Polymers102,0303
Non-polymers14,99823
Water55831
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_5551

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Components

#1: Protein Potassium channel TASK2 / Potassium channel / subfamily K / member 5 / TASK2 potassium channel


Mass: 38662.777 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Kcnk5 / Production host: Komagataella pastoris (fungus) / References: UniProt: Q9JK62
#2: Protein Apolipoprotein A-I / Apo-AI / ApoA-I / Apolipoprotein A1 / MSP1D1 scaffold protein


Mass: 24704.729 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: APOA1 / Production host: Escherichia coli (E. coli) / References: UniProt: P02647
#3: Chemical ChemComp-K / POTASSIUM ION


Mass: 39.098 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: K
#4: Chemical
ChemComp-PEE / 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine / DOPE


Mass: 744.034 Da / Num. of mol.: 20 / Source method: isolated from a natural source / Formula: C41H78NO8P / Comment: DOPE, phospholipid*YM
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 31 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestN
Has protein modificationN

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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: TASK-2 L127N in MSP1D1 nanodisc / Type: COMPLEX / Entity ID: #1-#2 / Source: MULTIPLE SOURCES
Molecular weightValue: 0.077 MDa / Experimental value: NO
Source (natural)Organism: Mus musculus (house mouse)
Source (recombinant)Organism: Komagataella pastoris (fungus)
Buffer solutionpH: 6.5
SpecimenEmbedding 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: TFS KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 1500 nm / Nominal defocus min: 500 nm
Image recordingElectron dose: 50 e/Å2 / Film or detector model: TFS FALCON 4i (4k x 4k)

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Processing

SoftwareName: PHENIX / Version: 1.20.1_4487 / Classification: refinement
EM software
IDNameVersionCategory
1RELIONparticle selection
2PHENIX1.21.2_5419model refinement
13cryoSPARC3D reconstruction
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 2.75 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 51195 / Symmetry type: POINT
RefinementHighest resolution: 2.75 Å
Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS)

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