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@ARTICLE{Rllen:821076,
      author       = {Röllen, Katrin and Granzin, Joachim and Panwalkar, Vineet
                      and Arinkin, Vladimir and Rani, Raj and Hartmann, Rudolf and
                      Krauss, Ulrich and Jaeger, Karl-Erich and Willbold, Dieter
                      and Batra-Safferling, Renu},
      title        = {{S}ignaling {S}tates of a {S}hort {B}lue-{L}ight
                      {P}hotoreceptor {P}rotein {P}p{SB}1-{LOV} {R}evealed from
                      {C}rystal {S}tructures and {S}olution {NMR} {S}pectroscopy},
      journal      = {Journal of molecular biology},
      volume       = {428},
      number       = {19},
      issn         = {0022-2836},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier},
      reportid     = {FZJ-2016-06320},
      pages        = {3721 - 3736},
      year         = {2016},
      abstract     = {Light–Oxygen–Voltage (LOV) domains represent the
                      photo-responsive domains of various blue-light photoreceptor
                      proteins and are widely distributed in plants, algae, fungi,
                      and bacteria. Here, we report the dark-state crystal
                      structure of PpSB1-LOV, a slow-reverting short LOV protein
                      from Pseudomonas putida that is remarkably different from
                      our previously published “fully light-adapted” structure
                      [1]. A direct comparison of the two structures provides
                      insight into the light-activated signaling mechanism. Major
                      structural differences involve a ~11 Å movement of the C
                      terminus in helix Jα, ~4 Å movement of Hβ–Iβ loop,
                      disruption of hydrogen bonds in the dimer interface, and a
                      ~29° rotation of chain-B relative to chain-A as compared to
                      the light-state dimer. Both crystal structures and solution
                      NMR data are suggestive of the key roles of a conserved
                      glutamine Q116 and the N-cap region consisting of
                      A′α–Aβ loop and the A′α helix in controlling the
                      light-activated conformational changes. The activation
                      mechanism proposed here for the PpSB1-LOV supports a rotary
                      switch mechanism and provides insights into the signal
                      propagation mechanism in naturally existing and artificial
                      LOV-based, two-component systems and regulators.},
      cin          = {ICS-6 / IMET},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-6-20110106 / I:(DE-Juel1)IMET-20090612},
      pnm          = {553 - Physical Basis of Diseases (POF3-553) / 581 -
                      Biotechnology (POF3-581)},
      pid          = {G:(DE-HGF)POF3-553 / G:(DE-HGF)POF3-581},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000384383400005},
      pubmed       = {pmid:27291287},
      doi          = {10.1016/j.jmb.2016.05.027},
      url          = {https://juser.fz-juelich.de/record/821076},
}