Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Active conformations of neuronal Na, K-ATPase isoforms and a disease-causing mutant.
Journal, issue, pages	Nat Commun, Vol. 17, Issue 1, Year 2026
Publish date	Jul 29, 2026
Authors	Mads Eskesen Christensen / Michael Habeck / Adriana Katz / Marlene Uglebjerg Fruergaard / Yoav Peleg / Uri Pick / Steven J D Karlish / Poul Nissen /
PubMed Abstract	Na,K-ATPases establish and maintain the vital electrochemical gradients for Na and K across animal cell membranes. The protein is a ternary complex composed of α, β and FXYD subunits, of which ...Na,K-ATPases establish and maintain the vital electrochemical gradients for Na and K across animal cell membranes. The protein is a ternary complex composed of α, β and FXYD subunits, of which isoforms that fine-tune transport properties are expressed in a tissue-specific fashion. Here we report cryo-EM structures under active ATPase turn-over conditions of the ubiquitously expressed human α1β1FXYD1 and neuron-specific α3β1FXYD1 isoform complexes and probe their specific functional and biophysical properties. The data provides an extensive insight into Na-transport of ATP-activated enzyme through four distinct conformational states, including a sodium-bound phosphoenzyme intermediate, denoted [Na]E2P. This conformation reveals a crucial structural change that precedes Na release in the inward to outward (E1P-E2P) transition, within the general context of the sequential, active transport mechanism. We discuss the mechanism of the physiologically important differentiation in Na affinity of α3 compared to α1, the co-operative Na binding at the ion-binding sites, and the mechanistic aspects of cytoplasmic ion gating and extracellular Na release. Finally we present the structures of a disease-causing mutant form of α3, associated with Alternating Hemiplegia of Childhood (Q140L). The mutation compromises a specific phospholipid-binding pocket and impedes polyunsaturated phospholipid-mediated stimulation of Na,K-ATPase activity.
External links	Nat Commun / PubMed:42669691 / PubMed Central
Methods	EM (single particle)
Resolution	2.8 - 3.78 Å
Structure data	54113 9ro9 EMDB-54113, PDB-9ro9: Human alpha3 Na+,K+-ATPase in the Na+-bound E1-ATP state Method: EM (single particle) / Resolution: 3.27 Å 54114 9roa EMDB-54114, PDB-9roa: Human alpha3 Na+,K+-ATPase in the Na+-occluded E1P-ADP state Method: EM (single particle) / Resolution: 3.08 Å 54115 9rod EMDB-54115, PDB-9rod: Human alpha3 Na+,K+-ATPase in the Na+-occluded E2P state Method: EM (single particle) / Resolution: 3.12 Å 54116 9roe EMDB-54116, PDB-9roe: Human alpha3 Na+,K+-ATPase in the outward open E2P state Method: EM (single particle) / Resolution: 2.94 Å 54117 9rof EMDB-54117, PDB-9rof: Human alpha3 Na+,K+-ATPase in the Na+-bound E1-ATP state obtained under turnover conditions Method: EM (single particle) / Resolution: 3.27 Å 54118 9rog EMDB-54118, PDB-9rog: Human alpha3 Na+,K+-ATPase in the Na+-occluded E1P-ADP state obtained under turnover conditions Method: EM (single particle) / Resolution: 2.8 Å 54119 9roh EMDB-54119, PDB-9roh: Human alpha3 Na+,K+-ATPase in the Na+-occluded E2P state obtained under turnover conditions Method: EM (single particle) / Resolution: 2.92 Å 54120 9roi EMDB-54120, PDB-9roi: Human alpha3 Na+,K+-ATPase in the K+-occluded E2P state obtained under turnover conditions Method: EM (single particle) / Resolution: 2.94 Å 54121 9roj EMDB-54121, PDB-9roj: Human alpha3 Q140L Na+,K+-ATPase in the Na+-bound E1 state Method: EM (single particle) / Resolution: 3.58 Å 54122 9rok EMDB-54122, PDB-9rok: Human alpha3 Q140L Na+,K+-ATPase in the Na+-occluded E1P-ADP state Method: EM (single particle) / Resolution: 3.78 Å 54123 9rol EMDB-54123, PDB-9rol: Human alpha3 Q140L Na+,K+-ATPase in the Na+-occluded E2P state Method: EM (single particle) / Resolution: 3.54 Å 54124 9rom EMDB-54124, PDB-9rom: Human alpha3 Q140L Na+,K+-ATPase in the outward open E2P state Method: EM (single particle) / Resolution: 3.6 Å 54125 9ron EMDB-54125, PDB-9ron: Human alpha1 Na+,K+-ATPase in the Na+-bound E1 state Method: EM (single particle) / Resolution: 3.41 Å 54126 9roo EMDB-54126, PDB-9roo: Human alpha1 Na+,K+-ATPase in the Na+-occluded E1P-ADP state Method: EM (single particle) / Resolution: 3.5 Å 54127 9rop EMDB-54127, PDB-9rop: Human alpha1 Na+,K+-ATPase in the Na+-occluded E2P state Method: EM (single particle) / Resolution: 3.24 Å 54128 9roq EMDB-54128, PDB-9roq: Human alpha1 Na+,K+-ATPase in the outward open E2P state Method: EM (single particle) / Resolution: 3.33 Å
Chemicals	ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying moleculeYM ChemComp-CLR: CHOLESTEROL ChemComp-MG: Unknown entry ChemComp-NA: Unknown entry ChemComp-NAG: 2-acetamido-2-deoxy-beta-D-glucopyranose ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying moleculeYM ChemComp-PO3: PHOSPHITE ION ChemComp-K: Unknown entry
Source	homo sapiens (human)
Keywords	METAL TRANSPORT / active ion transport / P-type ATPase / Na/K-ATPase / E1 / MEMBRANE PROTEIN / E1P / E2P