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@ARTICLE{Endres:188053,
      author       = {Endres, Stephan and Granzin, Joachim and Circolone, Franco
                      and Stadler, Andreas and Krauss, Ulrich and Drepper, Thomas
                      and Svensson, Vera and Knieps-Grünhagen, Esther and Wirtz,
                      Astrid and Cousin, Anneliese and Tielen, Petra and Willbold,
                      Dieter and Jaeger, Karl-Erich and Batra-Safferling, Renu},
      title        = {{S}tructure and function of a short {LOV} protein from the
                      marine phototrophic bacterium {D}inoroseobacter shibae},
      journal      = {BMC microbiology},
      volume       = {15},
      number       = {1},
      issn         = {1471-2180},
      address      = {London},
      publisher    = {BioMed Central},
      reportid     = {FZJ-2015-01531},
      pages        = {30},
      year         = {2015},
      abstract     = {BackgroundLight, oxygen, voltage (LOV) domains are widely
                      distributed in plants, algae, fungi, bacteria, and represent
                      the photo-responsive domains of various blue-light
                      photoreceptor proteins. Their photocycle involves the
                      blue-light triggered adduct formation between the C(4a) atom
                      of a non-covalently bound flavin chromophore and the sulfur
                      atom of a conserved cysteine in the LOV sensor domain. LOV
                      proteins show considerable variation in the structure of N-
                      and C-terminal elements which flank the LOV core domain, as
                      well as in the lifetime of the adduct state.ResultsHere, we
                      report the photochemical, structural and functional
                      characterization of DsLOV, a LOV protein from the
                      photoheterotrophic marine α-proteobacterium Dinoroseobacter
                      shibae which exhibits an average adduct state lifetime of
                      9.6 s at 20°C, and thus represents the fastest reverting
                      bacterial LOV protein reported so far. Mutational analysis
                      in D. shibae revealed a unique role of DsLOV in controlling
                      the induction of photopigment synthesis in the absence of
                      blue-light. The dark state crystal structure of DsLOV
                      determined at 1.5 Å resolution reveals a conserved core
                      domain with an extended N-terminal cap. The dimer interface
                      in the crystal structure forms a unique network of hydrogen
                      bonds involving residues of the N-terminus and the
                      β-scaffold of the core domain. The structure of
                      photoexcited DsLOV suggests increased flexibility in the
                      N-cap region and a significant shift in the Cα backbone of
                      β strands in the N- and C-terminal ends of the LOV core
                      domain.ConclusionsThe results presented here cover the
                      characterization of the unusual short LOV protein DsLOV from
                      Dinoroseobacter shibae including its regulatory function,
                      extremely fast dark recovery and an N-terminus mediated
                      dimer interface. Due to its unique photophysical, structural
                      and regulatory properties, DsLOV might thus serve as an
                      alternative model system for studying light perception by
                      LOV proteins and physiological responses in bacteria.},
      cin          = {Neutronenstreuung ; JCNS-1 / ICS-1 / IMET / ICS-6},
      ddc          = {570},
      cid          = {I:(DE-Juel1)JCNS-1-20110106 / I:(DE-Juel1)ICS-1-20110106 /
                      I:(DE-Juel1)IMET-20090612 / I:(DE-Juel1)ICS-6-20110106},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551) /
                      6G4 - Jülich Centre for Neutron Research (JCNS) (POF3-623)
                      / 6215 - Soft Matter, Health and Life Sciences (POF3-621) /
                      89581 - Biotechnology (POF2-89581)},
      pid          = {G:(DE-HGF)POF3-551 / G:(DE-HGF)POF3-6G4 /
                      G:(DE-HGF)POF3-6215 / G:(DE-HGF)POF2-89581},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000350256600003},
      doi          = {10.1186/s12866-015-0365-0},
      url          = {https://juser.fz-juelich.de/record/188053},
}