ArticleProceedings of the National Academy of Sciences of the United States of America2015
Simulating the function of sodium/proton antiporters.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Exploring the Activation Process of the Glycine Receptor.Journal of the American Chemical Society · 2024Article
- The Contribution of Hydrophobic Interactions to Conformational Changes of Inward/Outward Transmembrane Transport Proteins.Membranes · 2022Article
- An angular motion of a conserved four-helix bundle facilitates alternating access transport in the TtNapA and EcNhaA transporters.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Mechanism of the electroneutral sodium/proton antiporter PaNhaP from transition-path shooting.Nature communications · 2019Article
- ZnT2 is an electroneutral proton-coupled vesicular antiporter displaying an apparent stoichiometry of two protons per zinc ion.PLoS computational biology · 2019Article
- Demonstrating aspects of multiscale modeling by studying the permeation pathway of the human ZnT2 zinc transporter.PLoS computational biology · 2018Article
- Exploring the free-energy landscape of GPCR activation.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- On the control of the proton current in the voltage-gated proton channel Hv1.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Ligand-induced conformational dynamics of theProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Simulating the Function of the MjNhaP1 Transporter.The journal of physical chemistry. B · 2016Article
- Mechanism of pH-dependent activation of the sodium-proton antiporter NhaA.Nature communications · 2016Article
- The Physics and Physical Chemistry of Molecular Machines.Chemphyschem : a European journal of chemical physics and physical chemistry · 2016Review
- The Ec-NhaA antiporter switches from antagonistic to synergistic antiport upon a single point mutation.Scientific reports · 2016Article
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Authors and funding
2 authors.
Funding
Abstract
The molecular basis of the function of transporters is a problem of significant importance, and the emerging structural information has not yet been converted to a full understanding of the corresponding function. This work explores the molecular origin of the function of the bacterial Na+/H+ antiporter NhaA by evaluating the energetics of the Na+ and H+ movement and then using the resulting landscape in Monte Carlo simulations that examine two transport models and explore which model can reproduce the relevant experimental results. The simulations reproduce the observed transport features by a relatively simple model that relates the protein structure to its transporting function. Focusing on the two key aspartic acid residues of NhaA, D163 and D164, shows that the fully charged state acts as an Na+ trap and that the fully protonated one poses an energetic barrier that blocks the transport of Na+. By alternating between the former and latter states, mediated by the partially protonated protein, protons, and Na+ can be exchanged across the membrane at 2:1 stoichiometry. Our study provides a numerical validation of the need of large conformational changes for effective transport. Furthermore, we also yield a reasonable explanation for the observation that some mammalian transporters have 1:1 stoichiometry. The present coarse-grained model can provide a general way for exploring the function of transporters on a molecular level.
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