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@ARTICLE{Gushchin:834107,
      author       = {Gushchin, Ivan and Melnikov, Igor and Polovinkin, Vitaly
                      and Ishchenko, Andrii and Yuzhakova, Anastasia and Buslaev,
                      Pavel and Bourenkov, Gleb and Grudinin, Sergei and Round,
                      Ekaterina and Balandin, Taras and Borshchevskiy, Valentin
                      and Willbold, Dieter and Leonard, Gordon and Büldt, Georg
                      and Popov, Alexander and Gordeliy, Valentin},
      title        = {{M}echanism of transmembrane signaling by sensor histidine
                      kinases},
      journal      = {Science},
      volume       = {356},
      number       = {6342},
      issn         = {0036-8075},
      address      = {Washington, DC [u.a.]},
      publisher    = {American Association for the Advancement of Science},
      reportid     = {FZJ-2017-04108},
      pages        = {6345},
      year         = {2017},
      abstract     = {One of the major and essential classes of transmembrane
                      (TM) receptors, present in all domains of life, is sensor
                      histidine kinases (HKs), parts of two-component signaling
                      systems (TCS). The structural mechanisms of transmembrane
                      signaling by these sensors are poorly understood. We present
                      here crystal structures of the periplasmic sensor domain,
                      the TM domain and the cytoplasmic HAMP domain of the
                      Escherichia coli nitrate/nitrite sensor HK NarQ in the
                      ligand-bound and mutated ligand-free states. The structures
                      reveal that the ligand binding induces significant
                      rearrangements and piston-like shifts of TM helices. The
                      HAMP domain protomers undergo lever-like motions and convert
                      the piston-like motions into helical rotations. Our findings
                      provide the structural framework for complete understanding
                      of TM TCS signaling and for development of antimicrobial
                      treatments targeting TCS.},
      cin          = {ICS-6},
      ddc          = {500},
      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:000402871700044},
      pubmed       = {pmid:28522691},
      doi          = {10.1126/science.aah6345},
      url          = {https://juser.fz-juelich.de/record/834107},
}