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@ARTICLE{Arinkin:842277,
      author       = {Arinkin, Vladimir and Granzin, Joachim and Röllen, Katrin
                      and Krauss, Ulrich and Jaeger, Karl-Erich and Willbold,
                      Dieter and Batra-Safferling, Renu},
      title        = {{S}tructure of a {LOV} protein in apo-state and
                      implications for construction of {LOV}-based optical tools},
      journal      = {Scientific reports},
      volume       = {7},
      issn         = {2045-2322},
      address      = {London},
      publisher    = {Nature Publishing Group},
      reportid     = {FZJ-2018-00524},
      pages        = {42971 -},
      year         = {2017},
      abstract     = {Unique features of Light-Oxygen-Voltage (LOV) proteins like
                      relatively small size (~12–19 kDa), inherent modularity,
                      highly-tunable photocycle and oxygen-independent
                      fluorescence have lately been exploited for the generation
                      of optical tools. Structures of LOV domains reported so far
                      contain a flavin chromophore per protein molecule. Here we
                      report two new findings on the short LOV protein
                      $W619_1-LOV$ from Pseudomonas putida. First, the apo-state
                      crystal structure of $W619_1-LOV$ at 2.5 Å resolution
                      reveals conformational rearrangements in the secondary
                      structure elements lining the chromophore pocket including
                      elongation of the Fα helix, shortening of the Eα-Fα loop
                      and partial unfolding of the Eα helix. Second, the apo
                      $W619_1-LOV$ protein binds both natural and structurally
                      modified flavin chromophores. Remarkably different
                      photophysical and photochemical properties of $W619_1-LOV$
                      bound to 7-methyl-8-chloro-riboflavin (8-Cl-RF) and
                      lumichrome imply application of these variants as novel
                      optical tools as they offer advantages such as no adduct
                      state formation, and a broader choice of wavelengths for in
                      vitro studies.},
      cin          = {IMET / ICS-6},
      ddc          = {000},
      cid          = {I:(DE-Juel1)IMET-20090612 / I:(DE-Juel1)ICS-6-20110106},
      pnm          = {581 - Biotechnology (POF3-581) / 551 - Functional
                      Macromolecules and Complexes (POF3-551)},
      pid          = {G:(DE-HGF)POF3-581 / G:(DE-HGF)POF3-551},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:28211532},
      UT           = {WOS:000394486200001},
      doi          = {10.1038/srep42971},
      url          = {https://juser.fz-juelich.de/record/842277},
}