+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-27167 | |||||||||
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Title | Human alpha3 Na+/K+-ATPase in its K+-occluded state | |||||||||
Map data | Human alpha3 Na+/K+-ATPase in its K+-occluded state | |||||||||
Sample |
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Function / homology | Function and homology information neuron to neuron synapse / protein transport into plasma membrane raft / positive regulation of calcium:sodium antiporter activity / 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 ...neuron to neuron synapse / protein transport into plasma membrane raft / positive regulation of calcium:sodium antiporter activity / 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 / intracellular sodium ion homeostasis / regulation of cardiac muscle contraction by calcium ion signaling / positive regulation of ATP-dependent activity / relaxation of cardiac muscle / Basigin interactions / cellular response to steroid hormone stimulus / sodium ion transport / organelle membrane / neuronal cell body 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 ion transmembrane transport / sodium channel regulator activity / cardiac muscle contraction / Ion homeostasis / ATP metabolic process / T-tubule / neuron projection maintenance / 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 / cell adhesion / protein stabilization / 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 | single particle reconstruction / cryo EM / Resolution: 4.1 Å | |||||||||
Authors | Nguyen PT / Bai X | |||||||||
Funding support | United States, 2 items
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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
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_27167.map.gz | 62.6 MB | EMDB map data format | |
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Header (meta data) | emd-27167-v30.xml emd-27167.xml | 19.9 KB 19.9 KB | Display Display | EMDB header |
Images | emd_27167.png | 46.1 KB | ||
Others | emd_27167_half_map_1.map.gz emd_27167_half_map_2.map.gz | 52.2 MB 52.2 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-27167 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-27167 | HTTPS FTP |
-Validation report
Summary document | emd_27167_validation.pdf.gz | 786.4 KB | Display | EMDB validaton report |
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Full document | emd_27167_full_validation.pdf.gz | 786 KB | Display | |
Data in XML | emd_27167_validation.xml.gz | 12.3 KB | Display | |
Data in CIF | emd_27167_validation.cif.gz | 14.4 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-27167 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-27167 | HTTPS FTP |
-Related structure data
Related structure data | 8d3xMC 8d3uC 8d3vC 8d3wC 8d3yC M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_27167.map.gz / Format: CCP4 / Size: 67 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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Annotation | Human alpha3 Na+/K+-ATPase in its K+-occluded state | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.83 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: Human alpha3 Na+/K+-ATPase in its K+-occluded state
File | emd_27167_half_map_1.map | ||||||||||||
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Annotation | Human alpha3 Na+/K+-ATPase in its K+-occluded state | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Human alpha3 Na+/K+-ATPase in its K+-occluded state
File | emd_27167_half_map_2.map | ||||||||||||
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Annotation | Human alpha3 Na+/K+-ATPase in its K+-occluded state | ||||||||||||
Projections & Slices |
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Density Histograms |
-Sample components
-Entire : Na+/K+-ATPase
Entire | Name: Na+/K+-ATPase |
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Components |
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-Supramolecule #1: Na+/K+-ATPase
Supramolecule | Name: Na+/K+-ATPase / type: complex / Chimera: Yes / ID: 1 / Parent: 0 / Macromolecule list: #1-#2 |
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Source (natural) | Organism: Homo sapiens (human) |
Recombinant expression | Organism: Mammalian expression vector Flag-MCS-pcDNA3.1 (others) |
-Macromolecule #1: Sodium/potassium-transporting ATPase subunit beta-1
Macromolecule | Name: Sodium/potassium-transporting ATPase subunit beta-1 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 35.108258 KDa |
Recombinant expression | Organism: Mammalian expression vector Flag-MCS-pcDNA3.1 (others) |
Sequence | String: MARGKAKEEG SWKKFIWNSE KKEFLGRTGG SWFKILLFYV IFYGCLAGIF IGTIQVMLLT ISEFKPTYQD RVAPPGLTQI PQIQKTEIS FRPNDPKSYE AYVLNIVRFL EKYKDSAQRD DMIFEDCGDV PSEPKERGDF NHERGERKVC RFKLEWLGNC S GLNDETYG ...String: MARGKAKEEG SWKKFIWNSE KKEFLGRTGG SWFKILLFYV IFYGCLAGIF IGTIQVMLLT ISEFKPTYQD RVAPPGLTQI PQIQKTEIS FRPNDPKSYE AYVLNIVRFL EKYKDSAQRD DMIFEDCGDV PSEPKERGDF NHERGERKVC RFKLEWLGNC S GLNDETYG YKEGKPCIII KLNRVLGFKP KPPKNESLET YPVMKYNPNV LPVQCTGKRD EDKDKVGNVE YFGLGNSPGF PL QYYPYYG KLLQPKYLQP LLAVQFTNLT MDTEIRIECK AYGENIGYSE KDRFQGRFDV KIEVKS |
-Macromolecule #2: FXYD domain-containing ion transport regulator 6
Macromolecule | Name: FXYD domain-containing ion transport regulator 6 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 10.855645 KDa |
Recombinant expression | Organism: Mammalian expression vector Flag-MCS-pcDNA3.1 (others) |
Sequence | String: MATMELVLVF LCSLLAPMVL ASAAEKEKEM DPFHYDYQTL RIGGLVFAVV LFSVGILLIL SRRCKCSFNQ KPRAPGDEEA QVENLITAN ATEPQKAEN |
-Macromolecule #3: Sodium/potassium-transporting ATPase subunit alpha-3
Macromolecule | Name: Sodium/potassium-transporting ATPase subunit alpha-3 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO / EC number: Na+/K+-exchanging ATPase |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 111.864289 KDa |
Recombinant expression | Organism: Mammalian expression vector Flag-MCS-pcDNA3.1 (others) |
Sequence | String: MGDKKDDKDS PKKNKGKERR DLDDLKKEVA MTEHKMSVEE VCRKYNTDCV QGLTHSKAQE ILARDGPNAL TPPPTTPEWV KFCRQLFGG FSILLWIGAI LCFLAYGIQA GTEDDPSGDN LYLGIVLAAV VIITGCFSYY QEAKSSKIME SFKNMVPQQA L VIREGEKM ...String: MGDKKDDKDS PKKNKGKERR DLDDLKKEVA MTEHKMSVEE VCRKYNTDCV QGLTHSKAQE ILARDGPNAL TPPPTTPEWV KFCRQLFGG FSILLWIGAI LCFLAYGIQA GTEDDPSGDN LYLGIVLAAV VIITGCFSYY QEAKSSKIME SFKNMVPQQA L VIREGEKM QVNAEEVVVG DLVEIKGGDR VPADLRIISA HGCKVDNSSL TGESEPQTRS PDCTHDNPLE TRNITFFSTN CV EGTARGV VVATGDRTVM GRIATLASGL EVGKTPIAIE IEHFIQLITG VAVFLGVSFF ILSLILGYTW LEAVIFLIGI IVA NVPEGL LATVTVCLTL TAKRMARKNC LVKNLEAVET LGSTSTICSD KTGTLTQNRM TVAHMWFDNQ IHEADTTEDQ SGTS FDKSS HTWVALSHIA GLCNRAVFKG GQDNIPVLKR DVAGDASESA LLKCIELSSG SVKLMRERNK KVAEIPFNST NKYQL SIHE TEDPNDNRYL LVMKGAPERI LDRCSTILLQ GKEQPLDEEM KEAFQNAYLE LGGLGERVLG FCHYYLPEEQ FPKGFA FDC DDVNFTTDNL CFVGLMSMID PPRAAVPDAV GKCRSAGIKV IMVTGDHPIT AKAIAKGVGI ISEGNETVED IAARLNI PV SQVNPRDAKA CVIHGTDLKD FTSEQIDEIL QNHTEIVFAR TSPQQKLIIV EGCQRQGAIV AVTGDGVNDS PALKKADI G VAMGIAGSDV SKQAADMILL DDNFASIVTG VEEGRLIFDN LKKSIAYTLT SNIPEITPFL LFIMANIPLP LGTITILCI DLGTDMVPAI SLAYEAAESD IMKRQPRNPR TDKLVNERLI SMAYGQIGMI QALGGFFSYF VILAENGFLP GNLVGIRLNW DDRTVNDLE DSYGQQWTYE QRKVVEFTCH TAFFVSIVVV QWADLIICKT RRNSVFQQGM KNKILIFGLF EETALAAFLS Y CPGMDVAL RMYPLKPSWW FCAFPYSFLI FVYDEIRKLI LRRNPGGWVE KETYY |
-Macromolecule #4: TETRAFLUOROMAGNESATE(2-)
Macromolecule | Name: TETRAFLUOROMAGNESATE(2-) / type: ligand / ID: 4 / Number of copies: 1 / Formula: MF4 |
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Molecular weight | Theoretical: 100.299 Da |
Chemical component information | ChemComp-MF4: |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Concentration | 4 mg/mL |
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Buffer | pH: 7.4 |
Grid | Model: Quantifoil R1.2/1.3 / Material: GOLD / Mesh: 300 / Pretreatment - Type: GLOW DISCHARGE |
Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Specialist optics | Energy filter - Name: GIF Bioquantum / Energy filter - Slit width: 20 eV |
Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Detector mode: SUPER-RESOLUTION / Average electron dose: 60.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: OTHER / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.6 µm / Nominal defocus min: 1.6 µm |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |