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@ARTICLE{Nazarenko:866224,
      author       = {Nazarenko, Vera V. and Remeeva, Alina and Yudenko, Anna and
                      Kovalev, Kirill and Dubenko, Anton and Goncharov, Ivan M.
                      and Kuzmichev, Pavel and Rogachev, Andrey V. and Buslaev,
                      Pavel and Borshchevskiy, Valentin and Mishin, Alexey and
                      Dhoke, Gaurao V. and Schwaneberg, Ulrich and Davari, Mehdi
                      D. and Jaeger, Karl-Erich and Krauss, Ulrich and Gordeliy,
                      Valentin and Gushchin, Ivan},
      title        = {{A} thermostable flavin-based fluorescent protein from
                      {C}hloroflexus aggregans : a framework for ultra-high
                      resolution structural studies},
      journal      = {Photochemical $\&$ photobiological sciences},
      volume       = {18},
      number       = {7},
      issn         = {1474-9092},
      address      = {Cambridge},
      publisher    = {Royal Society of Chemistry},
      reportid     = {FZJ-2019-05390},
      pages        = {1793 - 1805},
      year         = {2019},
      abstract     = {Light-Oxygen-Voltage (LOV) domains are conserved parts of
                      photoreceptors in plants, bacteria and fungi that bind
                      flavins as chromophores and detect blue light. In the past,
                      LOV domain variants have been developed as fluorescent
                      reporter proteins (called flavin-based fluorescent proteins;
                      FbFPs), which due to their ability to fluoresce under
                      anaerobic conditions, fast folding kinetics and a small size
                      of ∼12–16 kDa are a promising reporter system for
                      quantitative real-time analysis of biological processes.
                      Here, we present a small thermostable flavin-based
                      fluorescent protein CagFbFP derived from a soluble LOV
                      domain-containing histidine kinase from the thermophilic
                      bacterium Chloroflexus aggregans. CagFbFP is composed of 107
                      amino acids with a molecular weight of 11.6 kDa and consists
                      only of the conserved LOV core domain. The protein is
                      thermostable with a melting point of about 68 °C. It
                      crystallizes easily and its crystals diffract to 1.07 Å.
                      Both the crystal structure and small angle scattering data
                      show that the protein is a dimer. Unexpectedly, glutamine
                      148, which in LOV photoreceptor proteins is the key residue
                      responsible for signal transduction, occupies two
                      conformations. Molecular dynamics simulations show that the
                      two conformations interconvert rapidly. The crystal
                      structure of the wild-type Chloroflexus aggregans LOV domain
                      determined at 1.22 Å resolution confirmed the presence of
                      two alternative conformations of the glutamine 148 side
                      chain. Overall, this protein, due to its stability and ease
                      of crystallization, appears to be a promising model for
                      ultra-high resolution structural studies of LOV domains and
                      for application as a fluorescent reporter.},
      cin          = {IMET / ICS-6 / IBG-1},
      ddc          = {620},
      cid          = {I:(DE-Juel1)IMET-20090612 / I:(DE-Juel1)ICS-6-20110106 /
                      I:(DE-Juel1)IBG-1-20101118},
      pnm          = {581 - Biotechnology (POF3-581)},
      pid          = {G:(DE-HGF)POF3-581},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:31116222},
      UT           = {WOS:000477947100017},
      doi          = {10.1039/C9PP00067D},
      url          = {https://juser.fz-juelich.de/record/866224},
}