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@ARTICLE{Arinkin:1023020,
      author       = {Arinkin, Vladimir and Granzin, Joachim and Jaeger,
                      Karl-Erich and Willbold, Dieter and Krauss, Ulrich and
                      Batra-Safferling, Renu},
      title        = {{C}onserved {S}ignal {T}ransduction {M}echanisms and {D}ark
                      {R}ecovery {K}inetic {T}uning in the {P}seudomonadaceae
                      {S}hort {L}ight, {O}xygen, {V}oltage ({LOV}) {P}rotein
                      {F}amily},
      journal      = {Journal of molecular biology},
      volume       = {436},
      number       = {5},
      issn         = {0022-2836},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier},
      reportid     = {FZJ-2024-01603},
      pages        = {168458 -},
      year         = {2024},
      abstract     = {Light-Oxygen-Voltage (LOV) flavoproteins transduce a light
                      signal into variable signaling outputs via a structural
                      rearrangement in the sensory core domain, which is then
                      relayed to fused effector domains via α-helical linker
                      elements. Short LOV proteins from Pseudomonadaceae consist
                      of a LOV sensory core and N- and C-terminal α-helices of
                      variable length, providing a simple model system to study
                      the molecular mechanism of allosteric activation. Here we
                      report the crystal structures of two LOV proteins from
                      Pseudomonas fluorescens - SBW25-LOV in the fully
                      light-adapted state and Pf5-LOV in the dark-state. In a
                      comparative analysis of the Pseudomonadaceae short LOVs, the
                      structures demonstrate light-induced rotation of the core
                      domains and splaying of the proximal A'α and Jα helices in
                      the N and C-termini, highlighting evidence for a conserved
                      signal transduction mechanism. Another distinguishing
                      feature of the Pseudomonadaceae short LOV protein family is
                      their highly variable dark recovery, ranging from seconds to
                      days. Understanding this variability is crucial for tuning
                      the signaling behavior of LOV-based optogenetic tools. At 37
                      °C, SBW25-LOV and Pf5-LOV exhibit adduct state lifetimes of
                      1470 min and 3.6 min, respectively. To investigate this
                      remarkable difference in dark recovery rates, we targeted
                      three residues lining the solvent channel entrance to the
                      chromophore pocket where we introduced mutations by
                      exchanging the non-conserved amino acids from SBW25-LOV into
                      Pf5-LOV and vice versa. Dark recovery kinetics of the
                      resulting mutants, as well as MD simulations and solvent
                      cavity calculations on the crystal structures suggest a
                      correlation between solvent accessibility and adduct
                      lifetime.},
      cin          = {IBI-7 / IMET},
      ddc          = {610},
      cid          = {I:(DE-Juel1)IBI-7-20200312 / I:(DE-Juel1)IMET-20090612},
      pnm          = {5241 - Molecular Information Processing in Cellular Systems
                      (POF4-524) / 2171 - Biological and environmental resources
                      for sustainable use (POF4-217)},
      pid          = {G:(DE-HGF)POF4-5241 / G:(DE-HGF)POF4-2171},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {38280482},
      UT           = {WOS:001218660600001},
      doi          = {10.1016/j.jmb.2024.168458},
      url          = {https://juser.fz-juelich.de/record/1023020},
}