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@ARTICLE{Gushchin:875097,
      author       = {Gushchin, Ivan and Orekhov, Philipp and Melnikov, Igor and
                      Polovinkin, Vitaly and Yuzhakova, Anastasia and Gordeliy,
                      Valentin},
      title        = {{S}ensor {H}istidine {K}inase {N}ar{Q} {A}ctivates via
                      {H}elical {R}otation, {D}iagonal {S}cissoring, and
                      {E}ventually {P}iston-{L}ike {S}hifts},
      journal      = {International journal of molecular sciences},
      volume       = {21},
      number       = {9},
      issn         = {1422-0067},
      address      = {Basel},
      publisher    = {Molecular Diversity Preservation International},
      reportid     = {FZJ-2020-01800},
      pages        = {3110 -},
      year         = {2020},
      abstract     = {Membrane-embedded sensor histidine kinases (HKs) and
                      chemoreceptors are used ubiquitously by bacteria and archaea
                      to percept the environment, and are often crucial for their
                      survival and pathogenicity. The proteins can transmit the
                      signal from the sensor domain to the catalytic kinase domain
                      reliably over the span of several hundreds of angstroms, and
                      regulate the activity of the cognate response regulator
                      proteins, with which they form two-component signaling
                      systems (TCSs). Several mechanisms of transmembrane signal
                      transduction in TCS receptors have been proposed, dubbed
                      (swinging) piston, helical rotation, and diagonal
                      scissoring. Yet, despite decades of studies, there is no
                      consensus on whether these mechanisms are common for all TCS
                      receptors. Here, we extend our previous work on Escherichia
                      coli nitrate/nitrite sensor kinase NarQ. We determined a
                      crystallographic structure of the sensor-TM-HAMP fragment of
                      the R50S mutant, which, unexpectedly, was found in a
                      ligand-bound-like conformation, despite an inability to bind
                      nitrate. Subsequently, we reanalyzed the structures of the
                      ligand-free and ligand-bound NarQ and NarX sensor domains,
                      and conducted extensive molecular dynamics simulations of
                      ligand-free and ligand-bound wild type and mutated NarQ.
                      Based on the data, we show that binding of nitrate to NarQ
                      causes, first and foremost, helical rotation and diagonal
                      scissoring of the α-helices at the core of the sensor
                      domain. These conformational changes are accompanied by a
                      subtle piston-like motion, which is amplified by a switch in
                      the secondary structure of the linker between the sensor and
                      TM domains. We conclude that helical rotation, diagonal
                      scissoring, and piston are simply different degrees of
                      freedom in coiled-coil proteins and are not mutually
                      exclusive in NarQ, and likely in other nitrate sensors and
                      TCS proteins as well.},
      cin          = {IBI-7},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {552 - Engineering Cell Function (POF3-552)},
      pid          = {G:(DE-HGF)POF3-552},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:32354084},
      UT           = {WOS:000535581700081},
      doi          = {10.3390/ijms21093110},
      url          = {https://juser.fz-juelich.de/record/875097},
}