ArticleProceedings of the National Academy of Sciences of the United States of America2012
Cryo-EM structure of gastric H+,K+-ATPase with a single occupied cation-binding site.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 38 citations in OpenAlex.
- Structural and mutational insights define ERMA as the ER MgScience advances · 2026Article
- Identification of common genes associated with diabetic nephropathy and diabetic retinopathy.Frontiers in cell and developmental biology · 2026Article
- Convergent gene losses and pseudogenizations in multiple lineages of stomachless fishes.Communications biology · 2024Article
- Bioinformatic Study of Possible Acute Regulation of Acid Secretion in the Stomach.The Journal of membrane biology · 2024Article
- The NaThe Journal of biological chemistry · 2022Article
- Gastric proton pump with two occluded KNature communications · 2021Article
- A single KeLife · 2019Article
- Structure of the human plasma membrane CaNature communications · 2018Article
- KScientific reports · 2018Article
- Crystal structures of the gastric proton pump.Nature · 2018Article
- The cryo-EM structure of gastric HScientific reports · 2017Article
- Glutamate Water Gates in the Ion Binding Pocket of NaScientific reports · 2017Article
- Arginine substitution of a cysteine in transmembrane helix M8 converts Na+,K+-ATPase to an electroneutral pump similar to H+,K+-ATPase.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- P2C-Type ATPases and Their Regulation.Molecular neurobiology · 2016Review
- Human Type IV P-type ATPases That Work as Plasma Membrane Phospholipid Flippases and Their Regulation by Caspase and Calcium.The Journal of biological chemistry · 2016Article
- Parameter estimation for mathematical models of a nongastric H+(Na+)-K(+)(NH4+)-ATPase.American journal of physiology. Renal physiology · 2015Article
- Metal Fluoride Inhibition of a P-type H+ Pump: STABILIZATION OF THE PHOSPHOENZYME INTERMEDIATE CONTRIBUTES TO POST-TRANSLATIONAL PUMP ACTIVATION.The Journal of biological chemistry · 2015Article
- Human SLC4A11-C functions as a DIDS-stimulatable H⁺(OH⁻) permeation pathway: partial correction of R109H mutant transport.American journal of physiology. Cell physiology · 2015Article
- Systematic comparison of molecular conformations of H+,K+-ATPase reveals an important contribution of the A-M2 linker for the luminal gating.The Journal of biological chemistry · 2014Article
- Carbon sandwich preparation preserves quality of two-dimensional crystals for cryo-electron microscopy.Microscopy (Oxford, England) · 2013Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Gastric H(+),K(+)-ATPase is responsible for gastric acid secretion. ATP-driven H(+) uptake into the stomach is efficiently accomplished by the exchange of an equal amount of K(+), resulting in a luminal pH close to 1. Because of the limited free energy available for ATP hydrolysis, the stoichiometry of transported cations is thought to vary from 2H(+)/2K(+) to 1H(+)/1K(+) per hydrolysis of one ATP molecule as the luminal pH decreases, although direct evidence for this hypothesis has remained elusive. Here, we show, using the phosphate analog aluminum fluoride (AlF) and a K(+) congener (Rb(+)), the 8-Å resolution structure of H(+),K(+)-ATPase in the transition state of dephosphorylation, (Rb(+))E2~AlF, which is distinct from the preceding Rb(+)-free E2P state. A strong density located in the transmembrane cation-binding site of (Rb(+))E2~AlF highly likely represents a single bound Rb(+) ion, which is clearly different from the Rb(+)-free E2AlF or K(+)-bound (K(+))E2~AlF structures. Measurement of radioactive (86)Rb(+) binding suggests that the binding stoichiometry varies depending on the pH, and approximately half of the amount of Rb(+) is bound under acidic crystallization conditions compared with at a neutral pH. These data represent structural and biochemical evidence for the 1H(+)/1K(+)/1ATP transport mode of H(+),K(+)-ATPase, which is a prerequisite for generation of the 10(6)-fold proton gradient in terms of thermodynamics. Together with the released E2P-stabilizing interaction between the β subunit's N terminus and the P domain observed in the (Rb(+))E2~AlF structure, we propose a refined vectorial transport model of H(+),K(+)-ATPase, which must prevail against the highly acidic state of the gastric lumen.
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