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@ARTICLE{Gushchin:279612,
      author       = {Gushchin, Ivan and Shevchenko, Vitaly and Polovinkin,
                      Vitaly and Borshchevskiy, Valentin and Buslaev, Pavel and
                      Bamberg, Ernst and Gordeliy, Valentin},
      title        = {{S}tructure of the light-driven sodium pump {KR}2 and its
                      implications for optogenetics},
      journal      = {The FEBS journal},
      volume       = {283},
      number       = {7},
      issn         = {1742-464X},
      address      = {Oxford [u.a.]},
      publisher    = {Wiley-Blackwell},
      reportid     = {FZJ-2015-07496},
      pages        = {1232–1238},
      year         = {2016},
      abstract     = {A key and common process present in the organisms from all
                      the domains of life is the maintenance of the ion gradient
                      between inside and outside of the cell. The gradient is
                      generated by various active transporters, among which are
                      the light-driven ion pumps of the microbial rhodopsins
                      family. While the proton- 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) residues, unusual ion uptake cavity acting as a
                      selectivity filter and the unique N-terminal α-helix,
                      capping the ion release cavity, as well as unexpected
                      flexibility of the retinal binding pocket. The structures
                      also revealed pentamerization of KR2 and binding of sodium
                      ions at the interface. Finally, based on the structures, the
                      potassium-pumping KR2 variants have been designed, making
                      the findings even more important for optogenetic
                      applications. In this Structural Snapshot, we analyze the
                      implications of the structural findings for understanding of
                      the sodium translocation mechanism and application of the
                      pump and its mutants in optogenetics. This article is
                      protected by copyright. All rights reserved.This article is
                      protected by copyright. All rights reserved.},
      cin          = {ICS-6},
      ddc          = {540},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551)},
      pid          = {G:(DE-HGF)POF3-551},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000374010500004},
      pubmed       = {pmid:26535564},
      doi          = {10.1111/febs.13585},
      url          = {https://juser.fz-juelich.de/record/279612},
}