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@ARTICLE{Wojtowicz:811935,
      author       = {Wojtowicz, H. and Prochnicka-Chalufour, A. and de Amorim,
                      G. C. and Roudenko, O. and Simenel, C. and Malki, I. and
                      Pehau-Arnaudet, G. and Gubellini, F. and Koutsioumpas,
                      Alexandros and Perez, J. and Delepelaire, P. and Delepierre,
                      M. and Fronzes, R. and Izadi-Pruneyre, N.},
      title        = {{S}tructural basis of the signalling through a bacterial
                      membrane receptor {H}as{R} deciphered by an integrative
                      approach},
      journal      = {Biochemical journal},
      volume       = {473},
      number       = {14},
      issn         = {1470-8728},
      address      = {London},
      publisher    = {Portland Press79505},
      reportid     = {FZJ-2016-04249},
      pages        = {2239 - 2248},
      year         = {2016},
      abstract     = {Bacteria use diverse signalling pathways to adapt gene
                      expression to external stimuli. In Gram-negative bacteria,
                      the binding of scarce nutrients to membrane transporters
                      triggers a signalling process that up-regulates the
                      expression of genes of various functions, from uptake of
                      nutrient to production of virulence factors. Although
                      proteins involved in this process have been identified,
                      signal transduction through this family of transporters is
                      not well understood. In the present study, using an
                      integrative approach (EM, SAXS, X-ray crystallography and
                      NMR), we have studied the structure of the haem transporter
                      HasR captured in two stages of the signalling process, i.e.
                      before and after the arrival of signalling activators (haem
                      and its carrier protein). We show for the first time that
                      the HasR domain responsible for signal transfer: (i) is
                      highly flexible in two stages of signalling; (ii) extends
                      into the periplasm at approximately 70–90 Å (1 Å=0.1 nm)
                      from the HasR β-barrel; and (iii) exhibits local
                      conformational changes in response to the arrival of
                      signalling activators. These features would favour the
                      signal transfer from HasR to its cytoplasmic membrane
                      partners.},
      cin          = {JCNS (München) ; Jülich Centre for Neutron Science JCNS
                      (München) ; JCNS-FRM-II / Neutronenstreuung ; JCNS-1},
      ddc          = {540},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)JCNS-1-20110106},
      pnm          = {6G15 - FRM II / MLZ (POF3-6G15) / 6G4 - Jülich Centre for
                      Neutron Research (JCNS) (POF3-623)},
      pid          = {G:(DE-HGF)POF3-6G15 / G:(DE-HGF)POF3-6G4},
      experiment   = {EXP:(DE-MLZ)NOSPEC-20140101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000393707500022},
      pubmed       = {pmid:27208170},
      doi          = {10.1042/BCJ20160131},
      url          = {https://juser.fz-juelich.de/record/811935},
}