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@ARTICLE{Gordeliy:877435,
      author       = {Gordeliy, Valentin and Baeken, Christian and Balandin,
                      Taras},
      title        = {{C}rystal {S}tructure of the {N}112{A} {M}utant of the
                      {L}ight-{D}riven {S}odium {P}ump {KR}2},
      journal      = {Crystals},
      volume       = {10},
      number       = {6},
      issn         = {2073-4352},
      address      = {Basel},
      publisher    = {MDPI},
      reportid     = {FZJ-2020-02190},
      pages        = {496 -},
      year         = {2020},
      abstract     = {The light-driven sodium pump KR2, found in 2013 in the
                      marine bacteria Krokinobacter eikastus, serves as a model
                      protein for the studies of the sodium-pumping microbial
                      rhodopsins (NaRs). KR2 possesses a unique NDQ (N112, D116,
                      and Q123) set of the amino acid residues in the functionally
                      relevant positions, named the NDQ motif. The N112 was shown
                      to determine the Na+/H+ selectivity and pumping efficiency
                      of the protein. Thus, N112A mutation converts KR2 into an
                      outward proton pump. However, no structural data on the
                      functional conversions of the light-driven sodium pumps are
                      available at the moment. Here we present the crystal
                      structure of the N112A mutant of KR2 in the ground state at
                      the resolution of 2.4 Å. The structure revealed a minor
                      deflection in the central part of the helix C and a double
                      conformation of the L74 residue in the mutant. The
                      organization of the retinal Schiff base and neighboring
                      water molecules is preserved in the ground state of
                      KR2-N112A. The presented data provide structural insights
                      into the effects of the alterations of the characteristic
                      NDQ motif of NaRs. Our findings also demonstrate that for
                      the rational design of the KR2 variants with modified ion
                      selectivity for optogenetic applications, the structures of
                      the intermediate states of both the protein and its
                      functional variants are required.},
      cin          = {IBI-7},
      ddc          = {540},
      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},
      UT           = {WOS:000551177600001},
      doi          = {10.3390/cryst10060496},
      url          = {https://juser.fz-juelich.de/record/877435},
}