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  Multiconformation continuum electrostatics analysis of the NhaA Na+/H+ antiporter of Escherichia coli with functional implications

Olkhova, E., Hunte, C., Screpanti, E., Padan, E., & Michel, H. (2006). Multiconformation continuum electrostatics analysis of the NhaA Na+/H+ antiporter of Escherichia coli with functional implications. Proceedings of the National Academy of Sciences of the United States of America, 103(8), 2629-2634. doi:10.1073/pnas.0510914103.

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Datensatz-Permalink: https://hdl.handle.net/11858/00-001M-0000-0024-D93F-B Versions-Permalink: https://hdl.handle.net/21.11116/0000-000B-A260-1
Genre: Zeitschriftenartikel

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 Urheber:
Olkhova, Elena1, Autor           
Hunte, Carola1, Autor           
Screpanti, Emanuela1, Autor           
Padan, Etana2, Autor
Michel, Hartmut1, Autor                 
Affiliations:
1Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
2Department of Biological Chemistry, Alexander Silberman Institute of Life Sciences, Hebrew University of Jerusalem, Jerusalem 91904, Israel, ou_persistent22              

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Schlagwörter: hydrogen-bonded networks; multiconformers; water binding sites
 Zusammenfassung: Sodium proton antiporters are essential enzymes that catalyze the exchange of sodium ions for protons across biological membranes. Protonations and deprotonations of individual amino acid residues and of clusters formed by these residues play an important role in activating these enzymes and in the mechanism of transport. We have used multiconformation continuum electrostatics method to investigate the protonation states of residues in the sodium proton exchanger NhaA from Escherichia coli, the structure of which has been determined recently by x-ray crystallography. Our calculations identify four clusters of electrostatically tightly interacting residues as well as long-range interactions between residues required for activation. The importance of many of these residues has been demonstrated by the characterization of site-directed mutants. A number of residues with extreme pKa values, including several of the “pH sensor,” can only undergo protonation/deprotonation reactions subsequent to conformational changes. The results of the calculations provide valuable information on the activation of the antiporter and the role of individual amino acid residues, and provide a solid framework for further experiments.

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Sprache(n): eng - English
 Datum: 2005-12-202006-02-132006-02-21
 Publikationsstatus: Erschienen
 Seiten: 6
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1073/pnas.0510914103
 Art des Abschluß: -

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Titel: Proceedings of the National Academy of Sciences of the United States of America
  Andere : Proc. Acad. Sci. USA
  Andere : Proc. Acad. Sci. U.S.A.
  Andere : Proceedings of the National Academy of Sciences of the USA
  Kurztitel : PNAS
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: Washington, D.C. : National Academy of Sciences
Seiten: - Band / Heft: 103 (8) Artikelnummer: - Start- / Endseite: 2629 - 2634 Identifikator: ISSN: 0027-8424
CoNE: https://pure.mpg.de/cone/journals/resource/954925427230