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@ARTICLE{Gushchin:202104,
      author       = {Gushchin, Ivan and Chervakov, Pavel and Kuzmichev, Pavel
                      and Popov, Alexander N and Round, Ekaterina and
                      Borshchevskiy, Valentin and Ishchenko, Andrii and
                      Petrovskaya, Lada and Chupin, Vladimir and Dolgikh, Dmitry A
                      and Arseniev, Alexander S and Arseniev, Alexander A and
                      Kirpichnikov, Mikhail and Gordeliy, Valentin},
      title        = {{S}tructural insights into the proton pumping by unusual
                      proteorhodopsin from nonmarine bacteria},
      journal      = {Proceedings of the National Academy of Sciences of the
                      United States of America},
      volume       = {110},
      number       = {31},
      issn         = {1091-6490},
      address      = {Washington, DC},
      publisher    = {National Acad. of Sciences},
      reportid     = {FZJ-2015-04393},
      pages        = {12631 - 12636},
      year         = {2013},
      abstract     = {Light-driven proton pumps are present in many organisms.
                      Here, we present a high-resolution structure of a
                      proteorhodopsin from a permafrost bacterium, Exiguobacterium
                      sibiricum rhodopsin (ESR). Contrary to the proton pumps of
                      known structure, ESR possesses three unique features. First,
                      ESR's proton donor is a lysine side chain that is situated
                      very close to the bulk solvent. Second, the α-helical
                      structure in the middle of the helix F is replaced by 3(10)-
                      and π-helix-like elements that are stabilized by the
                      Trp-154 and Asn-224 side chains. This feature is
                      characteristic for the proteorhodopsin family of proteins.
                      Third, the proton release region is connected to the bulk
                      solvent by a chain of water molecules already in the ground
                      state. Despite these peculiarities, the positions of water
                      molecule and amino acid side chains in the immediate Schiff
                      base vicinity are very well conserved. These features make
                      ESR a very unusual proton pump. The presented structure
                      sheds light on the large family of proteorhodopsins, for
                      which structural information was not available previously.},
      keywords     = {Bacterial Proteins (NLM Chemicals) / proteorhodopsin (NLM
                      Chemicals) / Rhodopsin (NLM Chemicals)},
      cin          = {ICS-6},
      ddc          = {000},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {452 - Structural Biology (POF2-452)},
      pid          = {G:(DE-HGF)POF2-452},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:23872846},
      pmc          = {pmc:PMC3732926},
      UT           = {WOS:000322441500040},
      doi          = {10.1073/pnas.1221629110},
      url          = {https://juser.fz-juelich.de/record/202104},
}