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@ARTICLE{Remeeva:904327,
      author       = {Remeeva, Alina and Nazarenko, Vera V. and Kovalev, Kirill
                      and Goncharov, Ivan M. and Yudenko, Anna and Astashkin,
                      Roman and Gordeliy, Valentin and Gushchin, Ivan},
      title        = {{I}nsights into the mechanisms of light‐oxygen‐voltage
                      domain color tuning from a set of high‐resolution
                      {X}‐ray structures},
      journal      = {Proteins},
      volume       = {89},
      number       = {8},
      issn         = {0887-3585},
      address      = {New York, NY},
      publisher    = {Wiley-Liss},
      reportid     = {FZJ-2021-05897},
      pages        = {1005 - 1016},
      year         = {2021},
      abstract     = {Light-oxygen-voltage (LOV) domains are widespread
                      photosensory modules that can be used in fluorescence
                      microscopy, optogenetics and controlled production of
                      reactive oxygen species. All of the currently known LOV
                      domains have absorption maxima in the range of ~440 to
                      ~450 nm, and it is not clear whether they can be shifted
                      significantly using mutations. Here, we have generated a
                      panel of LOV domain variants by mutating the key
                      chromophore-proximal glutamine aminoacid of a thermostable
                      flavin based fluorescent protein CagFbFP (Gln148) to
                      asparagine, aspartate, glutamate, histidine, lysine and
                      arginine. Absorption spectra of all of the mutants are
                      blue-shifted, with the maximal shift of 8 nm observed for
                      the Q148H variant. While CagFbFP and its Q148N/D/E variants
                      are not sensitive to pH, Q148H/K/R reveal a moderate red
                      shift induced byacidic pH. To gain further insight, we
                      determined high resolution crystal structures of all of the
                      mutants studied at the resolutions from 1.07 Å for Q148D
                      to 1.63 Å for Q148R. Whereas in some of the variants, the
                      aminoacid 148 remains in the vicinity of the flavin, in
                      Q148K, Q148R and partially Q148D, the C-terminus of the
                      protein unlatches and the side chain of the residue 148 is
                      reoriented away from the chromophore. Our results explain
                      the absence of color shifts from replacing Gln148 with
                      charged aminoacids and pave the way for rational design of
                      color-shifted flavin based fluorescent proteins.},
      cin          = {IBI-7},
      ddc          = {570},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {5241 - Molecular Information Processing in Cellular Systems
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {33774867},
      UT           = {WOS:000635931200001},
      doi          = {10.1002/prot.26078},
      url          = {https://juser.fz-juelich.de/record/904327},
}