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@ARTICLE{Rajasekar:317072,
      author       = {Rajasekar, Karthik V. and Lovering, Andrew L. and Dancea,
                      Felician and Scott, David J. and Harris, Sarah A. and
                      Bingle, Lewis E. H. and Roessle, Manfred and Thomas,
                      Christopher M. and Hyde, Eva I. and White, Scott A.},
      title        = {{F}lexibility of {K}or{A}, a plasmid-encoded, global
                      transcription regulator, in the presence and the absence of
                      its operator},
      journal      = {Nucleic acids symposium series},
      volume       = {44},
      number       = {10},
      issn         = {1362-4962},
      address      = {Oxford},
      publisher    = {Oxford Univ. Press},
      reportid     = {PUBDB-2017-00413},
      pages        = {4947 - 4956},
      year         = {2016},
      abstract     = {The IncP (Incompatibility group P) plasmids are important
                      carriers in the spread of antibiotic resistance across
                      Gram-negative bacteria. Gene expression in the IncP-1
                      plasmids is stringently controlled by a network of four
                      global repressors, KorA, KorB, TrbA and KorC interacting
                      cooperatively. Intriguingly, KorA and KorB can act as
                      co-repressors at varying distances between their operators,
                      even when they are moved to be on opposite sides of the DNA.
                      KorA is a homodimer with the 101-amino acid subunits,
                      folding into an N-terminal DNA-binding domain and a
                      C-terminal dimerization domain. In this study, we have
                      determined the structures of the free KorA repressor and two
                      complexes each bound to a 20-bp palindromic DNA duplex
                      containing its consensus operator sequence. Using a
                      combination of X-ray crystallography, nuclear magnetic
                      resonance spectroscopy, SAXS and molecular dynamics
                      calculations, we show that the linker between the two
                      domains is very flexible and the protein remains highly
                      mobile in the presence of DNA. This flexibility allows the
                      DNA-binding domains of the dimer to straddle the operator
                      DNA on binding and is likely to be important in cooperative
                      binding to KorB. Unexpectedly, the C-terminal domain of KorA
                      is structurally similar to the dimerization domain of the
                      tumour suppressor p53.},
      cin          = {EMBL},
      ddc          = {540},
      cid          = {I:(DE-H253)EMBL-20120731},
      pnm          = {899 - ohne Topic (POF3-899)},
      pid          = {G:(DE-HGF)POF3-899},
      experiment   = {EXP:(DE-H253)DORISIII(machine)-20150101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000379754600043},
      pubmed       = {pmid:27016739},
      doi          = {10.1093/nar/gkw191},
      url          = {https://bib-pubdb1.desy.de/record/317072},
}