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@ARTICLE{Palm:448261,
      author       = {Palm, Gottfried Julius and Buchholz, Ina and Werten,
                      Sebastiaan and Girbardt, Britta and Berndt, Leona and
                      Delcea, Mihaela and Hinrichs, Winfried},
      title        = {{T}hermodynamics, cooperativity and stability of the
                      tetracycline repressor ({T}et{R}) upon tetracycline binding},
      journal      = {Biochimica et biophysica acta / Proteins and proteomics},
      volume       = {1868},
      number       = {6},
      issn         = {1570-9639},
      address      = {Amsterdam [u.a.]},
      reportid     = {PUBDB-2020-03359},
      pages        = {140404},
      year         = {2020},
      abstract     = {Allosteric regulation of the Tet repressor (TetR) homodimer
                      relies on tetracycline binding that abolishes the affinity
                      for the DNA operator. Previously, interpretation of circular
                      dichroism data called for unfolding of the α-helical
                      DNA-binding domains in absence of binding to DNA or
                      tetracycline. Our small angle X-ray scattering of TetR(D) in
                      solution contradicts this unfolding as a physiological
                      process. Instead, in the core domain crystal structures
                      analyses show increased immobilisation of helix α9 and two
                      C-terminal turns of helix α8 upon tetracycline binding.
                      Tetracycline complexes of TetR(D) and four single-site
                      alanine variants were characterised by isothermal titration
                      calorimetry, fluorescence titration, X-ray crystal
                      structures, and melting curves. Five crystal structures
                      confirm that Thr103 is a key residue for the allosteric
                      events of induction, with the T103A variant lacking
                      induction by any tetracycline. The T103A variant shows
                      anti-cooperative inducer binding, and a melting curve of the
                      tetracycline complex different to TetR(D) and other
                      variants. For the N82A variant inducer binding is clearly
                      anti-cooperative but triggers the induced conformation.},
      cin          = {EMBL-User},
      ddc          = {570},
      cid          = {I:(DE-H253)EMBL-User-20120814},
      pnm          = {6G3 - PETRA III (POF3-622)},
      pid          = {G:(DE-HGF)POF3-6G3},
      experiment   = {EXP:(DE-H253)P-P12-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:32114262},
      UT           = {WOS:000527000700004},
      doi          = {10.1016/j.bbapap.2020.140404},
      url          = {https://bib-pubdb1.desy.de/record/448261},
}