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@ARTICLE{Gordeliy:865288,
      author       = {Gordeliy, Valentin and Bratanov, Dmitry and Kovalev, Kirill
                      and Machtens, Jan-Philipp and Astashkin, Roman and Chizhov,
                      Igor and Soloviov, Dmytro and Volkov, Dmytro and Polovinkin,
                      Vitaly and Zabelskii, Dmitrii and Mager, Thomas and
                      Gushchin, Ivan and Rokitskaya, Tatyana and Antonenko, Yuri
                      and Alekseev, Alexey and Shevchenko, Vitaly and Yutin,
                      Natalya and Rosselli, Riccardo and Baeken, Christian and
                      Borshchevskiy, Valentin and Bourenkov, Gleb and Popov,
                      Alexander and Balandin, Taras and Büldt, Georg and
                      Manstein, Dietmar J. and Rodriguez-Valera, Francisco and
                      Fahlke, Christoph and Bamberg, Ernst and Koonin, Eugene},
      title        = {{U}nique structure and function of viral rhodopsins},
      journal      = {Nature Communications},
      volume       = {10},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Nature Publishing Group UK},
      reportid     = {FZJ-2019-04808},
      pages        = {4939},
      year         = {2019},
      abstract     = {Recently, two groups of rhodopsin genes were identified in
                      large double-stranded DNA viruses. The structure and
                      function of viral rhodopsins are unknown. We present
                      functional characterization and high-resolution structure of
                      an Organic Lake Phycodnavirus rhodopsin II (OLPVRII) of
                      group 2. It forms a pentamer, with a symmetrical,
                      bottle-like central channel with the narrow vestibule in the
                      cytoplasmic part covered by a ring of 5 arginines, whereas 5
                      phenylalanines form a hydrophobic barrier in its exit. The
                      proton donor E42 is placed in the helix B. The structure is
                      unique among the known rhodopsins. Structural and functional
                      data and molecular dynamics suggest that OLPVRII might be a
                      light-gated pentameric ion channel analogous to pentameric
                      ligand-gated ion channels, however, future patch clamp
                      experiments should prove this directly. The data shed light
                      on a fundamentally distinct branch of rhodopsins and may
                      contribute to the understanding of virus-host interactions
                      in ecologically important marine protists.},
      cin          = {ICS-6 / ICS-4 / JARA-HPC},
      ddc          = {500},
      cid          = {I:(DE-Juel1)ICS-6-20110106 / I:(DE-Juel1)ICS-4-20110106 /
                      $I:(DE-82)080012_20140620$},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551) /
                      MOLECULAR MODELLING OF BIFUNCTIONAL MEMBRANE TRANSPORT
                      PROTEINS $(jics40_20130501)$ / Screening the impurity
                      effects on transport properties in topological materials
                      $(jara0191_20181101)$ / Molecular dynamics of the SLC26
                      family of ion channels and transporters
                      $(jara0177_20171101)$},
      pid          = {G:(DE-HGF)POF3-551 / $G:(DE-Juel1)jics40_20130501$ /
                      $G:(DE-Juel1)jara0191_20181101$ /
                      $G:(DE-Juel1)jara0177_20171101$},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:31666521},
      UT           = {WOS:000493275600013},
      doi          = {10.1038/s41467-019-12718-0},
      url          = {https://juser.fz-juelich.de/record/865288},
}