ArticleNature communications2015
Sequential substitution of K(+) bound to Na(+),K(+)-ATPase visualized by X-ray crystallography.
Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Impact of Time, Temperature, and Conformational Changes on the Characterization of Cardiotonic Steroid-NaThe Journal of membrane biology · 2026Review
- Simplified Method for Kinetic and Thermodynamic Screening of Cardiotonic Steroids through the KMolecular pharmacology · 2024Article
- NaInternational journal of molecular sciences · 2024Review
- Circular RNA and intervertebral disc degeneration: unravelling mechanisms and implications.Frontiers in molecular biosciences · 2023Review
- Structural basis for gating mechanism of the human sodium-potassium pump.Nature communications · 2022Article
- The NaThe Journal of biological chemistry · 2022Article
- Structures of prokaryotic ubiquitin-like protein Pup in complex with depupylase Dop reveal the mechanism of catalytic phosphate formation.Nature communications · 2021Article
- In vitro proof of concept studies of radiotoxicity from Auger electron-emitter thallium-201.EJNMMI research · 2021Article
- Rapid-Onset Dystonia-Parkinsonism Phenotype Consistency for a Novel Variant ofNeurology. Genetics · 2021Article
- Multiscale Simulations of Biological Membranes: The Challenge To Understand Biological Phenomena in a Living Substance.Chemical reviews · 2019Article
- Na/K Pump Mutations Associated with Primary Hyperaldosteronism Cause Loss of Function.Biochemistry · 2019Article
- Protein Interaction and Na/K-ATPase-Mediated Signal Transduction.Molecules (Basel, Switzerland) · 2017Review
- Assessing heterogeneity in oligomeric AAA+ machines.Cellular and molecular life sciences : CMLS · 2017Review
- Article
- Molecular Mechanisms of Enzyme Activation by Monovalent Cations.The Journal of biological chemistry · 2016Review
- Article
- Isolation, crystallization and crystal structure determination of bovine kidney Na(+),K(+)-ATPase.Acta crystallographica. Section F, Structural biology communications · 2016Article
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Authors and funding
4 authors.
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Abstract
Na(+),K(+)-ATPase transfers three Na(+) from the cytoplasm into the extracellular medium and two K(+) in the opposite direction per ATP hydrolysed. The binding and release of Na(+) and K(+) are all thought to occur sequentially. Here we demonstrate by X-ray crystallography of the ATPase in E2·MgF4(2-)·2K(+), a state analogous to E2·Pi·2K(+), combined with isotopic measurements, that the substitution of the two K(+) with congeners in the extracellular medium indeed occurs at different rates, substantially faster at site II. An analysis of thermal movements of protein atoms in the crystal shows that the M3-M4E helix pair opens and closes the ion pathway leading to the extracellular medium, allowing K(+) at site II to be substituted first. Taken together, these results indicate that site I K(+) is the first cation to bind to the empty cation-binding sites after releasing three Na(+).
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