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@ARTICLE{Circolone:20004,
      author       = {Circolone, F. and Granzin, J. and Jentzsch, K. and Drepper,
                      T. and Jaeger, K.E. and Willbold, D. and Krauss, U. and
                      Batra-Safferling, R.},
      title        = {{S}tructural basis for the slow dark recovery of a
                      full-length {LOV} protein from {P}seudomonas putida},
      journal      = {Journal of molecular biology},
      volume       = {417},
      issn         = {0022-2836},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier},
      reportid     = {PreJuSER-20004},
      pages        = {362 - 374},
      year         = {2012},
      note         = {The authors wish to thank Georg Buldt for continuous
                      generous support and the scientists at beamline ID23-2 at
                      the ESRF (Grenoble, France). Part of this work has been
                      funded by the Deutsche Forschungsgemeinschaft within the
                      GRK1166 "Biocatalysis in Non-Conventional Media".},
      comment      = {.},
      booktitle     = {.},
      abstract     = {Blue-light photoreceptors containing
                      light–oxygen–voltage (LOV) domains regulate a myriad of
                      different physiological responses in both eukaryotes and
                      prokaryotes. Their light sensitivity is intricately linked
                      to the photochemistry of the non-covalently bound flavin
                      mononucleotide (FMN) chromophore that forms a covalent
                      adduct with a conserved cysteine residue in the LOV domain
                      upon illumination with blue light. All LOV domains undergo
                      the same primary photochemistry leading to adduct formation;
                      however, considerable variation is found in the lifetime of
                      the adduct state that varies from seconds to several hours.
                      The molecular mechanism underlying this variation among the
                      structurally conserved LOV protein family is not well
                      understood. Here, we describe the structural
                      characterization of PpSB1-LOV, a very slow cycling
                      full-length LOV protein from the Gram-negative bacterium
                      Pseudomonas putida KT2440. Its crystal structure reveals a
                      novel dimer interface that is mediated by N- and C-terminal
                      auxiliary structural elements and a unique cluster of four
                      arginine residues coordinating with the FMN-phosphate
                      moiety. Site-directed mutagenesis of two arginines (R61 and
                      R66) in PpSB1-LOV resulted in acceleration of the dark
                      recovery reaction approximately by a factor of 280. The
                      presented structural and biochemical data suggest a direct
                      link between structural features and the slow dark recovery
                      observed for PpSB1-LOV. The overall structural arrangement
                      of PpSB1-LOV, together with a complementary phylogenetic
                      analysis, highlights a common ancestry of bacterial LOV
                      photoreceptors and Per-ARNT-Sim chemosensors.},
      keywords     = {Bacterial Proteins: chemistry / Crystallography, X-Ray /
                      Flavin Mononucleotide: chemistry / Light / Photoreceptors,
                      Microbial: chemistry / Protein Structure, Tertiary /
                      Pseudomonas putida: metabolism / Bacterial Proteins (NLM
                      Chemicals) / Photoreceptors, Microbial (NLM Chemicals) /
                      Flavin Mononucleotide (NLM Chemicals) / J (WoSType)},
      cin          = {ICS-6},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {Funktion und Dysfunktion des Nervensystems / BioSoft:
                      Makromolekulare Systeme und biologische
                      Informationsverarbeitung},
      pid          = {G:(DE-Juel1)FUEK409 / G:(DE-Juel1)FUEK505},
      shelfmark    = {Biochemistry $\&$ Molecular Biology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:22326872},
      UT           = {WOS:000302446600007},
      doi          = {10.1016/j.jmb.2012.01.056},
      url          = {https://juser.fz-juelich.de/record/20004},
}