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@ARTICLE{Zabelskii:893762,
      author       = {Zabelskii, Dmitrii and Dmitrieva, Natalia and Volkov,
                      Oleksandr and Shevchenko, Vitaly and Kovalev, Kirill and
                      Balandin, Taras and Soloviov, Dmytro and Astashkin, Roman
                      and Zinovev, Egor and Alekseev, Alexey and Round, Ekaterina
                      and Polovinkin, Vitaly and Chizhov, Igor and Rogachev,
                      Andrey and Okhrimenko, Ivan and Borshchevskiy, Valentin and
                      Chupin, Vladimir and Büldt, Georg and Yutin, Natalia and
                      Bamberg, Ernst and Koonin, Eugene and Gordeliy, Valentin},
      title        = {{S}tructure-based insights into evolution of rhodopsins},
      journal      = {Communications biology},
      volume       = {4},
      number       = {1},
      issn         = {2399-3642},
      address      = {London},
      publisher    = {Springer Nature},
      reportid     = {FZJ-2021-02817},
      pages        = {821},
      year         = {2021},
      abstract     = {Rhodopsins, most of which are proton pumps generating
                      transmembrane electrochemical proton gradients, span all
                      three domains of life, are abundant in the biosphere, and
                      could play a crucial role in the early evolution of life on
                      earth. Whereas archaeal and bacterial proton pumps are among
                      the best structurally characterized proteins, rhodopsins
                      from unicellular eukaryotes have not been well
                      characterized. To fill this gap in the current understanding
                      of the proton pumps and to gain insight into the evolution
                      of rhodopsins using a structure-based approach, we performed
                      a structural and functional analysis of the light-driven
                      proton pump LR (Mac) from the pathogenic fungus
                      Leptosphaeria maculans. The first high-resolution structure
                      of fungi rhodopsin and its functional properties reveal the
                      striking similarity of its membrane part to archaeal but not
                      to bacterial rhodopsins. We show that an unusually long
                      N-terminal region stabilizes the protein through direct
                      interaction with its extracellular loop (ECL2). We compare
                      to our knowledge all available structures and sequences of
                      outward light-driven proton pumps and show that eukaryotic
                      and archaeal proton pumps, most likely, share a common
                      ancestor.},
      cin          = {IBI-1},
      ddc          = {570},
      cid          = {I:(DE-Juel1)IBI-1-20200312},
      pnm          = {5241 - Molecular Information Processing in Cellular Systems
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {34193947},
      UT           = {WOS:000671710700003},
      doi          = {10.1038/s42003-021-02326-4},
      url          = {https://juser.fz-juelich.de/record/893762},
}