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@ARTICLE{Kovalev:875138,
      author       = {Kovalev, Kirill and Volkov, D. and Astashkin, R. and
                      Alekseev, Alexey and Gushchin, I. and Haro-Moreno, J. M. and
                      Chizhov, I. and Siletsky, S. and Mamedov, M. and Rogachev,
                      A. and Balandin, T. and Borshchevskiy, Valentin and Popov,
                      A. and Bourenkov, G. and Bamberg, E. and Rodriguez-Valera,
                      F. and Büldt, G. and Gordeliy, V.},
      title        = {{H}igh-resolution structural insights into the
                      heliorhodopsin family},
      journal      = {Proceedings of the National Academy of Sciences of the
                      United States of America},
      volume       = {117},
      number       = {8},
      issn         = {1091-6490},
      address      = {Washington, DC},
      publisher    = {National Acad. of Sciences},
      reportid     = {FZJ-2020-01830},
      pages        = {4131 - 4141},
      year         = {2020},
      abstract     = {Rhodopsins are the most abundant light-harvesting proteins.
                      A new family of rhodopsins, heliorhodopsins (HeRs), has
                      recently been discovered. Unlike in the known rhodopsins, in
                      HeRs the N termini face the cytoplasm. The function of HeRs
                      remains unknown. We present the structures of the bacterial
                      HeR-48C12 in two states at the resolution of 1.5 Å, which
                      highlight its remarkable difference from all known
                      rhodopsins. The interior of HeR’s extracellular part is
                      completely hydrophobic, while the cytoplasmic part comprises
                      a cavity (Schiff base cavity [SBC]) surrounded by charged
                      amino acids and containing a cluster of water molecules,
                      presumably being a primary proton acceptor from the Schiff
                      base. At acidic pH, a planar triangular molecule (acetate)
                      is present in the SBC. Structure-based bioinformatic
                      analysis identified 10 subfamilies of HeRs, suggesting their
                      diverse biological functions. The structures and available
                      data suggest an enzymatic activity of HeR-48C12 subfamily
                      and their possible involvement in fundamental redox
                      biological processes.},
      cin          = {IBI-7},
      ddc          = {500},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {552 - Engineering Cell Function (POF3-552)},
      pid          = {G:(DE-HGF)POF3-552},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:32034096},
      UT           = {WOS:000516771500038},
      doi          = {10.1073/pnas.1915888117},
      url          = {https://juser.fz-juelich.de/record/875138},
}