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@ARTICLE{Tamulaitiene:205427,
      author       = {Tamulaitiene, G. and Silanskas, A. and Grazulis, S. and
                      Zaremba, M. and Siksnys, V.},
      title        = {{C}rystal {S}tructure of the {R}-{P}rotein of the
                      {M}ultisubunit {ATP}-{D}ependent {R}estriction
                      {E}ndonuclease {N}go{AVII}},
      journal      = {Nucleic acids symposium series},
      volume       = {42},
      number       = {22},
      issn         = {1362-4962},
      address      = {Oxford},
      publisher    = {Oxford Univ. Press},
      reportid     = {PUBDB-2015-00004},
      pages        = {14022 - 14030},
      year         = {2014},
      note         = {OA},
      abstract     = {The restriction endonuclease (REase) NgoAVII iscomposed of
                      two proteins, R.NgoAVII and N.NgoAVII,and shares features of
                      both Type II restriction en-zymes and Type I/III
                      ATP-dependent restriction en-zymes (see accompanying paper
                      Zaremba et al.,2014). Here we present crystal structures of
                      theR.NgoAVII apo-protein and the R.NgoAVII C-terminaldomain
                      bound to a specific DNA. R.NgoAVII is com-posed of two
                      domains: an N-terminal nucleolytic PLDdomain; and a
                      C-terminal B3-like DNA-binding do-main identified previously
                      in BfiI and EcoRII REases,and in plant transcription
                      factors. Structural compar-ison of the B3-like domains of
                      R.NgoAVII, EcoRII, BfiIand the plant transcription factors
                      revealed a con-served DNA-binding surface comprised of N-
                      andC-arms that together grip the DNA. The C-arms
                      ofR.NgoAVII, EcoRII, BfiI and plant B3 domains are sim-ilar
                      in size, but the R.NgoAVII N-arm which makes themajority of
                      the contacts to the target site is muchlonger. The overall
                      structures of R.NgoAVII and BfiIare similar; however, whilst
                      BfiI has stand-alone cat-alytic activity, R.NgoAVII requires
                      an auxiliary cog-nate N.NgoAVII protein and ATP hydrolysis
                      in or-der to cleave DNA at the target site. The structureswe
                      present will help formulate future experiments toexplore the
                      molecular mechanisms of intersubunitcrosstalk that control
                      DNA cleavage by R.NgoAVIIand related endonucleases.},
      cin          = {EMBL-User},
      ddc          = {540},
      cid          = {I:(DE-H253)EMBL-User-20120814},
      pnm          = {PETRA Beamline P13 (POF2-54G14)},
      pid          = {G:(DE-H253)POF2-P13-20130405},
      experiment   = {EXP:(DE-H253)P-P13-20150101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000347916900056},
      pubmed       = {pmid:25429979},
      doi          = {10.1093/nar/gku1237},
      url          = {https://bib-pubdb1.desy.de/record/205427},
}