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@ARTICLE{Kovalev:874981,
      author       = {Kovalev, Kirill and Astashkin, Roman and Gushchin, Ivan and
                      Orekhov, Philipp and Volkov, Dmytro and Zinovev, Egor and
                      Marin, Egor and Rulev, Maksim and Alekseev, Alexey and
                      Royant, Antoine and Carpentier, Philippe and Vaganova,
                      Svetlana and Zabelskii, Dmitrii and Baeken, Christian and
                      Sergeev, Ilya and Balandin, Taras and Bourenkov, Gleb and
                      Carpena, Xavier and Boer, Roeland and Maliar, Nina and
                      Borshchevskiy, Valentin and Büldt, Georg and Bamberg, Ernst
                      and Gordeliy, Valentin},
      title        = {{M}olecular mechanism of light-driven sodium pumping},
      journal      = {Nature Communications},
      volume       = {11},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Nature Publishing Group UK},
      reportid     = {FZJ-2020-01746},
      pages        = {2137},
      year         = {2020},
      abstract     = {The light-driven sodium-pumping rhodopsin KR2 from
                      Krokinobacter eikastus is the only non-proton cation active
                      transporter with demonstrated potential for optogenetics.
                      However, the existing structural data on KR2 correspond
                      exclusively to its ground state, and show no sodium inside
                      the protein, which hampers the understanding of
                      sodium-pumping mechanism. Here we present crystal structure
                      of the O-intermediate of the physiologically relevant
                      pentameric form of KR2 at the resolution of 2.1 Å,
                      revealing a sodium ion near the retinal Schiff base,
                      coordinated by N112 and D116 of the characteristic NDQ
                      triad. We also obtained crystal structures of D116N and H30A
                      variants, conducted metadynamics simulations and measured
                      pumping activities of putative pathway mutants to
                      demonstrate that sodium release likely proceeds alongside
                      Q78 towards the structural sodium ion bound between KR2
                      protomers. Our findings highlight the importance of
                      pentameric assembly for sodium pump function, and may be
                      used for rational engineering of enhanced optogenetic
                      tools.},
      cin          = {IBI-7},
      ddc          = {500},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551)},
      pid          = {G:(DE-HGF)POF3-551},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:32358514},
      UT           = {WOS:000531425700018},
      doi          = {10.1038/s41467-020-16032-y},
      url          = {https://juser.fz-juelich.de/record/874981},
}