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@ARTICLE{Firczuk:205697,
      author       = {Firczuk, M. and Wojciechowski, Marek and Czapinska,
                      Honorata and Bochtler, Matthias},
      title        = {{DNA} intercalation without flipping in the specific
                      {T}ha{I}-{DNA} complex},
      journal      = {Nucleic acids research},
      volume       = {39},
      number       = {2},
      issn         = {0301-5610},
      address      = {Oxford},
      publisher    = {Oxford Univ. Press},
      reportid     = {PUBDB-2015-00257},
      pages        = {744 - 754},
      year         = {2011},
      abstract     = {The PD-(D/E)XK type II restriction endonucleaseThaI cuts
                      the target sequence CG/CG with bluntends. Here, we report
                      the 1.3 Å resolution structureof the enzyme in complex
                      with substrate DNA and asodium or calcium ion taking the
                      place of a catalyticmagnesium ion. The structure identifies
                      Glu54,Asp82 and Lys93 as the active site residues.
                      Thisagrees with earlier bioinformatic predictions andimplies
                      that the PD and (D/E)XK motifs in thesequence are
                      incidental. DNA recognition is veryunusual: the two Met47
                      residues of the ThaI dimerintercalate symmetrically into the
                      CG steps of thetarget sequence. They approach the DNA from
                      theminor groove side and penetrate the base stackentirely.
                      The DNA accommodates the intercalatingresidues without
                      nucleotide flipping by a doubling ofthe CG step rise to
                      twice its usual value, which isaccompanied by drastic
                      unwinding. Displacementof the Met47 side chains from the
                      base pairmidlines toward the downstream CG steps leadsto
                      large and compensating tilts of the first andsecond CG
                      steps. DNA intercalation by ThaI isunlike intercalation by
                      HincII, HinP1I or proteinsthat bend or repair DNA.},
      cin          = {DOOR},
      ddc          = {570},
      cid          = {I:(DE-H253)HAS-User-20120731},
      pnm          = {DORIS Beamline BW6 (POF2-54G13)},
      pid          = {G:(DE-H253)POF2-BW6-20130405},
      experiment   = {EXP:(DE-H253)D-BW6-20150101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000286675300037},
      pubmed       = {pmid:20861000},
      doi          = {10.1093/nar/gkq834},
      url          = {https://bib-pubdb1.desy.de/record/205697},
}