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  Structure of the light-driven sodium pump KR2 and its implications for optogenetics

Gushchin, I., Shevchenko, V., Polovinkin, V., Borshchevskiy, V., Buslaev, P., Bamberg, E., et al. (2016). Structure of the light-driven sodium pump KR2 and its implications for optogenetics. The FEBS Journal, 283(7), 1232-1238. doi:10.1111/febs.13585.

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Gushchin, Ivan1, 2, Autor
Shevchenko, Vitaly1, 2, Autor
Polovinkin, Vitaly1, 2, 3, 4, 5, Autor
Borshchevskiy, Valentin1, 2, Autor
Buslaev, Pavel2, Autor
Bamberg, Ernst6, Autor           
Gordeliy, Valentin1, 2, 3, 4, 5, Autor
Affiliations:
1Institute of Complex Systems (ICS), ICS-6: Structural Biochemistry, Research Centre Jülich, Germany, ou_persistent22              
2Moscow Institute of Physics and Technology, Dolgoprudniy, Russia, ou_persistent22              
3Institut de Biologie Structurale, Universit_e Grenoble Alpes, France, ou_persistent22              
4Institut de Biologie Structurale, Centre National de la Recherche Scientifique, Grenoble, France, ou_persistent22              
5Institut de Biologie Structurale, Direction des Sciences du Vivant, Commissariat à l’Énergie Atomique, Grenoble, France, ou_persistent22              
6Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society, ou_2068289              

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Schlagwörter: crystal structure; light-driven; microbial rhodopsins; optogenetics tools; potassium pump; sodium pump
 Zusammenfassung: A key and common process present in organisms from all domains of life is the maintenance of the ion gradient between the inside and the outside of the cell. The gradient is generated by various active transporters, among which are the light-driven ion pumps of the microbial rhodopsin family. Whereas the proton-pumping and anion-pumping rhodopsins have been known for a long time, the cation (sodium) pumps were described only recently. Following the discovery, high-resolution atomic structures of the pump KR2 were determined that revealed the complete ion translocation pathway, including the positions of the characteristic Asn-Asp-Gln (NDQ) triad, the unusual ion uptake cavity acting as a selectivity filter, the unique N-terminal α-helix, capping the ion release cavity, and unexpected flexibility of the retinal-binding pocket. The structures also revealed pentamerization of KR2 and binding of sodium ions at the interface. Finally, on the basis of the structures, potassium-pumping KR2 variants have been designed, making the findings even more important for optogenetic applications. In this Structural Snapshot, we analyse the implications of the structural findings for understanding the sodium translocation mechanism and application of the pump and its mutants in optogenetics.

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Sprache(n): eng - English
 Datum: 2015-09-082015-10-302016-04-052016-04
 Publikationsstatus: Erschienen
 Seiten: 7
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1111/febs.13585
 Art des Abschluß: -

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Titel: The FEBS Journal
  Andere : The Federation if European Biochemical Societies Journal
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: Wiley-Blackwell
Seiten: - Band / Heft: 283 (7) Artikelnummer: - Start- / Endseite: 1232 - 1238 Identifikator: ISSN: 1742-464X
CoNE: https://pure.mpg.de/cone/journals/resource/954925398485