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@ARTICLE{Ishchenko:827774,
      author       = {Ishchenko, Andrii and Round, E. and Borshchevskiy, Valentin
                      and Grudinin, S. and Gushchin, Ivan and Klare, J. P. and
                      Remeeva and Polovinkin, V. and Utrobin, P. and Balandin,
                      Taras and Engelhard, M. and Büldt, Georg and Gordeliy,
                      Valentin},
      title        = {{N}ew {I}nsights on {S}ignal {P}ropagation by {S}ensory
                      {R}hodopsin {II}/{T}ransducer {C}omplex},
      journal      = {Scientific reports},
      volume       = {7},
      issn         = {2045-2322},
      address      = {London},
      publisher    = {Nature Publishing Group},
      reportid     = {FZJ-2017-01878},
      pages        = {41811},
      year         = {2017},
      abstract     = {The complex of two membrane proteins, sensory rhodopsin II
                      (NpSRII) with its cognate transducer (NpHtrII), mediates
                      negative phototaxis in halobacteria N. pharaonis. Upon light
                      activation NpSRII triggers a signal transduction chain
                      homologous to the two-component system in eubacterial
                      chemotaxis. Here we report on crystal structures of the
                      ground and active M-state of the complex in the space group
                      I212121. We demonstrate that the relative orientation of
                      symmetrical parts of the dimer is parallel (“U”-shaped)
                      contrary to the gusset-like (“V”-shaped) form of the
                      previously reported structures of the NpSRII/NpHtrII complex
                      in the space group P21212, although the structures of the
                      monomers taken individually are nearly the same. Computer
                      modeling of the HAMP domain in the obtained “V”- and
                      “U”-shaped structures revealed that only the
                      “U”-shaped conformation allows for tight interactions of
                      the receptor with the HAMP domain. This is in line with
                      existing data and supports biological relevance of the
                      “U” shape in the ground state. We suggest that the
                      “V”-shaped structure may correspond to the active state
                      of the complex and transition from the “U” to the
                      “V”-shape of the receptor-transducer complex can be
                      involved in signal transduction from the receptor to the
                      signaling domain of NpHtrII.},
      cin          = {ICS-6},
      ddc          = {000},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551)},
      pid          = {G:(DE-HGF)POF3-551},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000393366600001},
      pubmed       = {pmid:28165484},
      doi          = {10.1038/srep41811},
      url          = {https://juser.fz-juelich.de/record/827774},
}