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@ARTICLE{Podoliak:607037,
      author       = {Podoliak, E. and Lamm, G. H. U. and Marin, E. and
                      Schellbach, A. V. and Fedotov, D. A. and Stetsenko, A. and
                      Asido, M. and Maliar, N. and Bourenkov, G. and Balandin, T.
                      and Baeken, C. and Astashkin, R. and Schneider, T. R. and
                      Bateman, A. and Wachtveitl, J. and Schapiro, I. and
                      Busskamp, V. and Guskov, A. and Gordeliy, V. and Alekseev,
                      A. and Kovalev, K.},
      title        = {{A} subgroup of light-driven sodium pumps with an
                      additional {S}chiff base counterion},
      journal      = {Nature Communications},
      volume       = {15},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Nature Publishing Group UK},
      reportid     = {PUBDB-2024-01742},
      pages        = {3119},
      year         = {2024},
      abstract     = {Light-driven sodium pumps (NaRs) are unique
                      ion-transporting microbial rhodopsins. The major group of
                      NaRs is characterized by an NDQ motif and has two aspartic
                      acid residues in the central region essential for sodium
                      transport. Here we identify a subgroup of the NDQ rhodopsins
                      bearing an additional glutamic acid residue in the close
                      vicinity to the retinal Schiff base. We thoroughly
                      characterize a member of this subgroup, namely the protein
                      ErNaR from Erythrobacter sp. HL-111 and show that the
                      additional glutamic acid results in almost complete loss of
                      pH sensitivity for sodium-pumping activity, which is in
                      contrast to previously studied NaRs. ErNaR is capable of
                      transporting sodium efficiently even at acidic pH levels.
                      X-ray crystallography and single particle cryo-electron
                      microscopy reveal that the additional glutamic acid residue
                      mediates the connection between the other two Schiff base
                      counterions and strongly interacts with the aspartic acid of
                      the characteristic NDQ motif. Hence, it reduces its pKa. Our
                      findings shed light on a subgroup of NaRs and might serve as
                      a basis for their rational optimization for optogenetics.},
      cin          = {EMBL-User / EMBL},
      ddc          = {500},
      cid          = {I:(DE-H253)EMBL-User-20120814 / I:(DE-H253)EMBL-20120731},
      pnm          = {6G3 - PETRA III (DESY) (POF4-6G3) / DFG project
                      G:(GEPRIS)390729940 - EXC 2067: Multiscale Bioimaging: Von
                      molekularen Maschinen zu Netzwerken erregbarer Zellen
                      (390729940) / DFG project G:(GEPRIS)390873048 - EXC 2151:
                      ImmunoSensation2 - the immune sensory system (390873048)},
      pid          = {G:(DE-HGF)POF4-6G3 / G:(GEPRIS)390729940 /
                      G:(GEPRIS)390873048},
      experiment   = {EXP:(DE-H253)P-P14-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:38600129},
      UT           = {WOS:001202408400026},
      doi          = {10.1038/s41467-024-47469-0},
      url          = {https://bib-pubdb1.desy.de/record/607037},
}