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  Ion Binding and Selectivity of the Na+/H+ Antiporter MjNhaP1 from Experiment and Simulation

Warnau, J., Wöhlert, D., Okazaki, K.-I., Yildiz, Ö., Gamiz-Hernandez, A. P., Kaila, V. R. I., et al. (2020). Ion Binding and Selectivity of the Na+/H+ Antiporter MjNhaP1 from Experiment and Simulation. The Journal of Physical Chemistry B, 124(2), 336-344. doi:10.1021/acs.jpcb.9b08552.

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 Creators:
Warnau, Judith1, 2, Author           
Wöhlert, David3, Author           
Okazaki, Kei-Ichi4, Author           
Yildiz, Özkan3, Author           
Gamiz-Hernandez, Ana P.2, 5, Author
Kaila, Ville R. I.2, 5, Author
Kühlbrandt, Werner3, Author           
Hummer, Gerhard1, 6, Author           
Affiliations:
1Department of Theoretical Biophysics, Max Planck Institute of Biophysics, Max Planck Society, ou_2068292              
2Department Chemie, Technische Universität München, Garching, Germany, ou_persistent22              
3Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068291              
4Department of Theoretical and Computational Molecular Science, Institute for Molecular Science, National Institutes of Natural Science, Okazaki, Japan, ou_persistent22              
5Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden, ou_persistent22              
6Insitute of Biophysics, Goethe University Frankfurt, Frankfurt am Main, Germany, ou_persistent22              

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 Abstract: Cells employ membrane-embedded antiporter proteins to control their pH, salt concentration, and volume. The large family of cation/proton antiporters is dominated by Na+/H+ antiporters that exchange sodium ions against protons, but homologous K+/H+ exchangers have recently been characterized. We show experimentally that the electroneutral antiporter NhaP1 of Methanocaldococcus jannaschii (MjNhaP1) is highly selective for Na+ ions. We then characterize the ion selectivity in both the inward-open and outward-open states of MjNhaP1 using classical molecular dynamics simulations, free energy calculations, and hybrid quantum/classical (QM/MM) simulations. We show that MjNhaP1 is highly selective for binding of Na+ over K+ in the inward-open state, yet it is only weakly selective in the outward-open state. These findings are consistent with the function of MjNhaP1 as a sodium-driven deacidifier of the cytosol that maintains a high cytosolic K+ concentration in environments of high salinity. By combining experiment and computation, we gain mechanistic insight into the Na+/H+ transport mechanism and help elucidate the molecular basis for ion selectivity in cation/proton exchangers.

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Language(s): eng - English
 Dates: 2019-11-162019-09-082019-12-162020-01-16
 Publication Status: Published in print
 Pages: 9
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1021/acs.jpcb.9b08552
BibTex Citekey: warnau_ion_2020
 Degree: -

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Title: The Journal of Physical Chemistry B
  Other : J. Phys. Chem. B
Source Genre: Journal
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Publ. Info: Washington, D.C. : American Chemical Society
Pages: - Volume / Issue: 124 (2) Sequence Number: - Start / End Page: 336 - 344 Identifier: ISSN: 1520-6106
CoNE: https://pure.mpg.de/cone/journals/resource/1000000000293370_1