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@ARTICLE{Schneidewind:864911,
      author       = {Schneidewind, Judith and Krause, Frank and Bocola, Marco
                      and Stadler, Andreas Maximilian and Davari, Mehdi D. and
                      Schwaneberg, Ulrich and Jaeger, Karl-Erich and Krauss,
                      Ulrich},
      title        = {{C}onsensus model of a cyanobacterial light-dependent
                      protochlorophyllide oxidoreductase in its pigment-free
                      apo-form and photoactive ternary complex},
      journal      = {Communications biology},
      volume       = {2},
      number       = {1},
      issn         = {2399-3642},
      address      = {London},
      publisher    = {Springer Nature},
      reportid     = {FZJ-2019-04514},
      pages        = {351},
      year         = {2019},
      abstract     = {Photosynthetic organisms employ two different enzymes for
                      the reduction of the C17 = C18 double bond of
                      protochlorophyllide (Pchlide), yielding the chlorophyll
                      precursor chlorophyllide. First, a nitrogenase-like,
                      light-independent (dark-operative) Pchlide oxidoreductase
                      and secondly, a light-dependent Pchlide oxidoreductase
                      (LPOR). For the latter enzyme, despite decades of research,
                      no structural information is available. Here, we use protein
                      structure modelling, molecular dynamics (MD) simulations
                      combined with multi-wavelength analytical
                      ultracentrifugation (MWA-AUC) and small angle X-ray
                      scattering (SAXS) experiments to derive a consensus model of
                      the LPOR apoprotein and the substrate/cofactor/LPOR ternary
                      complex. MWA-AUC and SAXS experiments independently
                      demonstrate that the apoprotein is monomeric, while ternary
                      complex formation induces dimerization. SAXS-guided
                      modelling studies provide a full-length model of the
                      apoprotein and suggest a tentative mode of dimerization for
                      the LPOR ternary complex, supported by published cross-link
                      constraints. Our study provides a first impression of the
                      LPOR structural organization.},
      cin          = {IBG-1 / IMET / JCNS-1 / ICS-1},
      ddc          = {570},
      cid          = {I:(DE-Juel1)IBG-1-20101118 / I:(DE-Juel1)IMET-20090612 /
                      I:(DE-Juel1)JCNS-1-20110106 / I:(DE-Juel1)ICS-1-20110106},
      pnm          = {581 - Biotechnology (POF3-581)},
      pid          = {G:(DE-HGF)POF3-581},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:31583285},
      UT           = {WOS:000488309300001},
      doi          = {10.1038/s42003-019-0590-4},
      url          = {https://juser.fz-juelich.de/record/864911},
}