ArticleThe Journal of biological chemistry2013
A conserved asparagine in a P-type proton pump is required for efficient gating of protons.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 20 citations in OpenAlex.
- Functional reconstitution of plant plasma membrane HScientific reports · 2025Article
- Sterol Extraction from Isolated Plant Plasma Membrane Vesicles Affects HBiomolecules · 2021Article
- Deciphering ion transport and ATPase coupling in the intersubunit tunnel of KdpFABC.Nature communications · 2021Article
- Homology modeling and in vivo functional characterization of the zinc permeation pathway in a heavy metal P-type ATPase.Journal of experimental botany · 2019Article
- 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
- Direct observation of proton pumping by a eukaryotic P-type ATPase.Science (New York, N.Y.) · 2016Article
- Dynamics of the Plasma Membrane Proton Pump.The Journal of membrane biology · 2015Article
- Article
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The minimal proton pumping machinery of the Arabidopsis thaliana P-type plasma membrane H(+)-ATPase isoform 2 (AHA2) consists of an aspartate residue serving as key proton donor/acceptor (Asp-684) and an arginine residue controlling the pKa of the aspartate. However, other important aspects of the proton transport mechanism such as gating, and the ability to occlude protons, are still unclear. An asparagine residue (Asn-106) in transmembrane segment 2 of AHA2 is conserved in all P-type plasma membrane H(+)-ATPases. In the crystal structure of the plant plasma membrane H(+)-ATPase, this residue is located in the putative ligand entrance pathway, in close proximity to the central proton donor/acceptor Asp-684. Substitution of Asn-106 resulted in mutant enzymes with significantly reduced ability to transport protons against a membrane potential. Sensitivity toward orthovanadate was increased when Asn-106 was substituted with an aspartate residue, but decreased in mutants with alanine, lysine, glutamine, or threonine replacement of Asn-106. The apparent proton affinity was decreased for all mutants, most likely due to a perturbation of the local environment of Asp-684. Altogether, our results demonstrate that Asn-106 is important for closure of the proton entrance pathway prior to proton translocation across the membrane.
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