+Open data
-Basic information
Entry | Database: PDB / ID: 8d3v | |||||||||
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Title | Human alpha3 Na+/K+-ATPase in its cytoplasmic side-open state | |||||||||
Components |
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Keywords | TRANSLOCASE/TRANSPORT PROTEIN / Na/K-ATPase / a3 / b1 / FXYD6 / occluded state / TRANSPORT PROTEIN / TRANSLOCASE-TRANSPORT PROTEIN complex | |||||||||
Function / homology | Function and homology information neuron to neuron synapse / protein transport into plasma membrane raft / positive regulation of potassium ion transmembrane transporter activity / positive regulation of P-type sodium:potassium-exchanging transporter activity / Na+/K+-exchanging ATPase / regulation of monoatomic ion transport / positive regulation of sodium ion export across plasma membrane / positive regulation of potassium ion import across plasma membrane / response to glycoside / membrane repolarization during cardiac muscle cell action potential ...neuron to neuron synapse / protein transport into plasma membrane raft / positive regulation of potassium ion transmembrane transporter activity / positive regulation of P-type sodium:potassium-exchanging transporter activity / Na+/K+-exchanging ATPase / regulation of monoatomic ion transport / positive regulation of sodium ion export across plasma membrane / positive regulation of potassium ion import across plasma membrane / response to glycoside / membrane repolarization during cardiac muscle cell action potential / photoreceptor inner segment membrane / regulation of resting membrane potential / establishment or maintenance of transmembrane electrochemical gradient / P-type sodium:potassium-exchanging transporter activity / steroid hormone binding / sodium:potassium-exchanging ATPase complex / membrane repolarization / sodium ion export across plasma membrane / cell communication by electrical coupling involved in cardiac conduction / intracellular potassium ion homeostasis / regulation of calcium ion transmembrane transport / intracellular sodium ion homeostasis / positive regulation of ATP-dependent activity / regulation of cardiac muscle contraction by calcium ion signaling / Basigin interactions / relaxation of cardiac muscle / cellular response to steroid hormone stimulus / sodium ion transport / neuronal cell body membrane / organelle membrane / potassium ion import across plasma membrane / monoatomic cation transmembrane transport / Ion transport by P-type ATPases / ATPase activator activity / intercalated disc / lateral plasma membrane / sperm flagellum / sodium channel regulator activity / sodium ion transmembrane transport / ATP metabolic process / cardiac muscle contraction / Ion homeostasis / neuron projection maintenance / T-tubule / photoreceptor inner segment / proton transmembrane transport / protein localization to plasma membrane / potassium ion transport / sarcolemma / intracellular calcium ion homeostasis / cellular response to amyloid-beta / extracellular vesicle / MHC class II protein complex binding / protein-folding chaperone binding / presynaptic membrane / amyloid-beta binding / protein-macromolecule adaptor activity / ATPase binding / regulation of gene expression / basolateral plasma membrane / postsynaptic membrane / Potential therapeutics for SARS / protein stabilization / cell adhesion / protein heterodimerization activity / apical plasma membrane / axon / innate immune response / neuronal cell body / glutamatergic synapse / synapse / protein kinase binding / Golgi apparatus / endoplasmic reticulum / ATP hydrolysis activity / extracellular exosome / ATP binding / membrane / metal ion binding / plasma membrane Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.4 Å | |||||||||
Authors | Nguyen, P.T. / Bai, X. | |||||||||
Funding support | United States, 2items
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Citation | Journal: Nat Commun / Year: 2022 Title: Structural basis for gating mechanism of the human sodium-potassium pump. Authors: Phong T Nguyen / Christine Deisl / Michael Fine / Trevor S Tippetts / Emiko Uchikawa / Xiao-Chen Bai / Beth Levine / Abstract: P2-type ATPase sodium-potassium pumps (Na/K-ATPases) are ion-transporting enzymes that use ATP to transport Na and K on opposite sides of the lipid bilayer against their electrochemical gradients to ...P2-type ATPase sodium-potassium pumps (Na/K-ATPases) are ion-transporting enzymes that use ATP to transport Na and K on opposite sides of the lipid bilayer against their electrochemical gradients to maintain ion concentration gradients across the membranes in all animal cells. Despite the available molecular architecture of the Na/K-ATPases, a complete molecular mechanism by which the Na and K ions access into and are released from the pump remains unknown. Here we report five cryo-electron microscopy (cryo-EM) structures of the human alpha3 Na/K-ATPase in its cytoplasmic side-open (E1), ATP-bound cytoplasmic side-open (E1•ATP), ADP-AlF trapped Na-occluded (E1•P-ADP), BeF trapped exoplasmic side-open (E2P) and MgF trapped K-occluded (E2•P) states. Our work reveals the atomically resolved structural detail of the cytoplasmic gating mechanism of the Na/K-ATPase. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 8d3v.cif.gz | 306.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb8d3v.ent.gz | 236.2 KB | Display | PDB format |
PDBx/mmJSON format | 8d3v.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 8d3v_validation.pdf.gz | 1.2 MB | Display | wwPDB validaton report |
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Full document | 8d3v_full_validation.pdf.gz | 1.2 MB | Display | |
Data in XML | 8d3v_validation.xml.gz | 42.4 KB | Display | |
Data in CIF | 8d3v_validation.cif.gz | 62.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/d3/8d3v ftp://data.pdbj.org/pub/pdb/validation_reports/d3/8d3v | HTTPS FTP |
-Related structure data
Related structure data | 27165MC 8d3uC 8d3wC 8d3xC 8d3yC M: map data used to model this data C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
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1 |
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-Components
#1: Protein | Mass: 111864.289 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ATP1A3 Production host: Mammalian expression vector Flag-MCS-pcDNA3.1 (others) References: UniProt: P13637, Na+/K+-exchanging ATPase |
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#2: Protein | Mass: 35108.258 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ATP1B1, ATP1B Production host: Mammalian expression vector Flag-MCS-pcDNA3.1 (others) References: UniProt: P05026 |
#3: Protein | Mass: 10855.645 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: FXYD6, UNQ521/PRO1056 Production host: Mammalian expression vector Flag-MCS-pcDNA3.1 (others) References: UniProt: Q9H0Q3 |
Has protein modification | Y |
-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
-Sample preparation
Component | Name: Na+/K+-ATPase / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT |
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Source (natural) | Organism: Homo sapiens (human) |
Source (recombinant) | Organism: Mammalian expression vector Flag-MCS-pcDNA3.1 (others) |
Buffer solution | pH: 7.4 |
Specimen | Conc.: 4 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Specimen support | Grid material: GOLD / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R1.2/1.3 |
Vitrification | Cryogen name: ETHANE |
-Electron microscopy imaging
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: OTHER |
Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2600 nm / Nominal defocus min: 1600 nm / Alignment procedure: COMA FREE |
Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
Image recording | Electron dose: 60 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
EM imaging optics | Energyfilter name: GIF Bioquantum / Energyfilter slit width: 20 eV |
-Processing
EM software |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
Particle selection | Num. of particles selected: 1970027 | ||||||||||||||||||||||||
Symmetry | Point symmetry: C1 (asymmetric) | ||||||||||||||||||||||||
3D reconstruction | Resolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 227349 / Symmetry type: POINT |