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@ARTICLE{Moukhametzianov:50688,
      author       = {Moukhametzianov, R. and Klare, J. P. and Efremov, R. and
                      Baeken, C. and Göppner, A. and Labahn, J. and Engelhard, M.
                      and Büldt, G. and Gordeliy, V. I.},
      title        = {{D}evelopment of the signal in sensory rhodopsin and its
                      transfer to the cognate transducer},
      journal      = {Nature},
      volume       = {440},
      issn         = {0028-0836},
      address      = {London [u.a.]},
      publisher    = {Nature Publising Group},
      reportid     = {PreJuSER-50688},
      pages        = {115 - 119},
      year         = {2006},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {The microbial phototaxis receptor sensory rhodopsin II
                      (NpSRII, also named phoborhodopsin) mediates the photophobic
                      response of the haloarchaeon Natronomonas pharaonis by
                      modulating the swimming behaviour of the bacterium. After
                      excitation by blue-green light NpSRII triggers, by means of
                      a tightly bound transducer protein (NpHtrII), a signal
                      transduction chain homologous with the two-component system
                      of eubacterial chemotaxis. Two molecules of NpSRII and two
                      molecules of NpHtrII form a 2:2 complex in membranes as
                      shown by electron paramagnetic resonance and X-ray structure
                      analysis. Here we present X-ray structures of the photocycle
                      intermediates K and late M (M2) explaining the evolution of
                      the signal in the receptor after retinal isomerization and
                      the transfer of the signal to the transducer in the complex.
                      The formation of late M has been correlated with the
                      formation of the signalling state. The observed structural
                      rearrangements allow us to propose the following mechanism
                      for the light-induced activation of the signalling complex.
                      On excitation by light, retinal isomerization leads in the K
                      state to a rearrangement of a water cluster that partly
                      disconnects two helices of the receptor. In the transition
                      to late M the changes in the hydrogen bond network proceed
                      further. Thus, in late M state an altered tertiary structure
                      establishes the signalling state of the receptor. The
                      transducer responds to the activation of the receptor by a
                      clockwise rotation of about 15 degrees of helix TM2 and a
                      displacement of this helix by 0.9 A at the cytoplasmic
                      surface.},
      keywords     = {Biological Evolution / Crystallography, X-Ray / Cytoplasm:
                      metabolism / Halobacteriaceae: chemistry / Halobacteriaceae:
                      cytology / Halobacteriaceae: metabolism / Halorhodopsins:
                      chemistry / Halorhodopsins: metabolism / Hydrogen Bonding /
                      Isomerism / Light Signal Transduction: physiology / Models,
                      Molecular / Protein Conformation / Sensory Rhodopsins:
                      chemistry / Sensory Rhodopsins: metabolism / Halorhodopsins
                      (NLM Chemicals) / Sensory Rhodopsins (NLM Chemicals) / J
                      (WoSType)},
      cin          = {IBI-2},
      ddc          = {070},
      cid          = {I:(DE-Juel1)VDB58},
      pnm          = {Funktion und Dysfunktion des Nervensystems},
      pid          = {G:(DE-Juel1)FUEK409},
      shelfmark    = {Multidisciplinary Sciences},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:16452929},
      UT           = {WOS:000235685700051},
      doi          = {10.1038/nature04520},
      url          = {https://juser.fz-juelich.de/record/50688},
}