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  Ligand-induced conformational dynamics of the Escherichia coli Na+/H+ antiporter NhaA revealed by hydrogen/deuterium exchange mass spectrometry

Eisinger, M. L., Dörrbaum, A. R., Michel, H., Padan, E., & Langer, J. D. (2017). Ligand-induced conformational dynamics of the Escherichia coli Na+/H+ antiporter NhaA revealed by hydrogen/deuterium exchange mass spectrometry. Proceedings of the National Academy of Sciences of the United States of America, 114(44), 11691-11696. doi:https://dx.doi.org/10.1073/pnas.1703422114.

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 Urheber:
Eisinger, Martin L.1, Autor           
Dörrbaum, Aline Ricarda1, 2, Autor           
Michel, Hartmut1, Autor           
Padan, Etana3, Autor
Langer, Julian David1, 2, Autor           
Affiliations:
1Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
2Synaptic Plasticity Department, Max Planck Institute for Brain Research, Max Planck Society, ou_2461710              
3Silberman Institute of Life Sciences, Hebrew University, Jerusalem 91904, Israel, ou_persistent22              

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Schlagwörter: NhaA; HDX-MS; conformational change; antiporter; membrane protein
 Zusammenfassung: Na+/H+ antiporters comprise a family of membrane proteins evolutionarily conserved in all kingdoms of life and play an essential role in cellular ion homeostasis. The NhaA crystal structure of Escherichia coli has become the paradigm for this class of secondary active transporters. However, structural data are only available at low pH, where NhaA is inactive. Here, we adapted hydrogen/deuterium-exchange mass spectrometry (HDX-MS) to analyze conformational changes in NhaA upon Li+ binding at physiological pH. Our analysis revealed a global conformational change in NhaA with two sets of movements around an immobile binding site. Based on these results, we propose a model for the ion translocation mechanism that explains previously controversial data for this antiporter. Furthermore, these findings contribute to our understanding of related human transporters that have been linked to various diseases.

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Sprache(n): eng - English
 Datum: 2017-10-312017-10-31
 Publikationsstatus: Erschienen
 Seiten: 6
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Art des Abschluß: -

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Titel: Proceedings of the National Academy of Sciences of the United States of America
  Andere : Proceedings of the National Academy of Sciences of the USA
  Andere : Proc. Acad. Sci. USA
  Andere : Proc. Acad. Sci. U.S.A.
  Kurztitel : PNAS
Genre der Quelle: Zeitschrift
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Affiliations:
Ort, Verlag, Ausgabe: Washington, D.C. : National Academy of Sciences
Seiten: - Band / Heft: 114 (44) Artikelnummer: - Start- / Endseite: 11691 - 11696 Identifikator: ISSN: 0027-8424
CoNE: https://pure.mpg.de/cone/journals/resource/954925427230