ArticleProceedings of the National Academy of Sciences of the United States of America2010
Structural identification of cation binding pockets in the plasma membrane proton pump.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Ion Changes and Signaling under Salt Stress in Wheat and Other Important Crops.Plants (Basel, Switzerland) · 2023Review
- Anionic Phospholipids Stimulate the Proton Pumping Activity of the Plant Plasma Membrane P-Type HInternational journal of molecular sciences · 2023Article
- Structure of the hexameric fungal plasma membrane proton pump in its autoinhibited state.Science advances · 2021Article
- Structural comparison of GLUT1 to GLUT3 reveal transport regulation mechanism in sugar porter family.Life science alliance · 2021Article
- Evolutionary and Functional Analysis of aFrontiers in plant science · 2019Article
- Improved Model of Proton Pump Crystal Structure Obtained by Interactive Molecular Dynamics Flexible Fitting Expands the Mechanistic Model for Proton Translocation in P-Type ATPases.Frontiers in physiology · 2017Article
- Inhibition of the Formation of the Spf1p Phosphoenzyme by Ca2.The Journal of biological chemistry · 2016Article
- 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
- Extracellular allosteric Na(+) binding to the Na(+),K(+)-ATPase in cardiac myocytes.Biophysical journal · 2013Article
- A conserved asparagine in a P-type proton pump is required for efficient gating of protons.The Journal of biological chemistry · 2013Article
- Ca2+ induces spontaneous dephosphorylation of a novel P5A-type ATPase.The Journal of biological chemistry · 2012Article
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The activity of P-type plasma membrane H(+)-ATPases is modulated by H(+) and cations, with K(+) and Ca(2+) being of physiological relevance. Using X-ray crystallography, we have located the binding site for Rb(+) as a K(+) congener, and for Tb(3+) and Ho(3+) as Ca(2+) congeners. Rb(+) is found coordinated by a conserved aspartate residue in the phosphorylation domain. A single Tb(3+) ion is identified positioned in the nucleotide-binding domain in close vicinity to the bound nucleotide. Ho(3+) ions are coordinated at two distinct sites within the H(+)-ATPase: One site is at the interface of the nucleotide-binding and phosphorylation domains, and the other is in the transmembrane domain toward the extracellular side. The identified binding sites are suggested to represent binding pockets for regulatory cations and a H(+) binding site for protons leaving the pump molecule. This implicates Ho(3+) as a novel chemical tool for identification of proton binding sites.
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