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@ARTICLE{Arinkin:890732,
      author       = {Arinkin, Vladimir and Granzin, Joachim and Krauss, Ulrich
                      and Jaeger, Karl-Erich and Willbold, Dieter and
                      Batra-Safferling, Renu},
      title        = {{S}tructural determinants underlying the adduct lifetime in
                      the {LOV} proteins of {P}seudomonas putida},
      journal      = {The FEBS journal},
      volume       = {288},
      number       = {16},
      issn         = {1742-4658},
      address      = {Oxford [u.a.]},
      publisher    = {Wiley-Blackwell},
      reportid     = {FZJ-2021-01155},
      pages        = {4955-4972},
      year         = {2021},
      abstract     = {The primary photochemistry is similar among the
                      flavin-bound sensory domains of light–oxygen–voltage
                      (LOV) photoreceptors, where upon blue-light illumination a
                      covalent adduct is formed on the microseconds time scale
                      between the flavin chromophore and a strictly conserved
                      cysteine residue. In contrast, the adduct-state decay
                      kinetics vary from seconds to days or longer. The molecular
                      basis for this variation among structurally conserved LOV
                      domains is not fully understood. Here, we selected
                      PpSB2-LOV, a fast-cycling (τrec 3.5 min, 20 °C) short LOV
                      protein from Pseudomonas putida that shares $67\%$ sequence
                      identity with a slow-cycling (τrec 2467 min, 20 °C)
                      homologous protein PpSB1-LOV. Based on the crystal structure
                      of the PpSB2-LOV in the dark state reported here, we used a
                      comparative approach, in which we combined structure and
                      sequence information with molecular dynamic (MD) simulations
                      to address the mechanistic basis for the vastly different
                      adduct-state lifetimes in the two homologous proteins. MD
                      simulations pointed toward dynamically distinct structural
                      region, which were subsequently targeted by site-directed
                      mutagenesis of PpSB2-LOV, where we introduced single- and
                      multisite substitutions exchanging them with the
                      corresponding residues from PpSB1-LOV. Collectively, the
                      data presented identify key amino acids on the Aβ-Bβ,
                      Eα-Fα loops, and the Fα helix, such as E27 and I66, that
                      play a decisive role in determining the adduct lifetime. Our
                      results additionally suggest a correlation between the
                      solvent accessibility of the chromophore pocket and
                      adduct-state lifetime. The presented results add to our
                      understanding of LOV signaling and will have important
                      implications in tuning the signaling behavior (on/off
                      kinetics) of LOV-based optogenetic tools.},
      cin          = {IBI-7},
      ddc          = {610},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {5244 - Information Processing in Neuronal Networks
                      (POF4-524) / 5241 - Molecular Information Processing in
                      Cellular Systems (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5244 / G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:33621443},
      UT           = {WOS:000628892400001},
      doi          = {10.1111/febs.15785},
      url          = {https://juser.fz-juelich.de/record/890732},
}