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@ARTICLE{Das:172498,
      author       = {Das, Uddipan and Pogenberg, Vivian and Tiruttani
                      Subhramanyam, Udaya Kumar and Matthias, Wilmanns and
                      Gourinath, Samudrala and Srinivana, Alagiri},
      title        = {{C}rystal structure of the {V}ap{BC}-15 complex from
                      {M}ycobacterium tuberculosis reveals a two-metal ion
                      dependent {PIN}-domain ribonuclease and a variable mode of
                      toxin-antitoxin assembly},
      journal      = {Journal of structural biology},
      volume       = {188},
      number       = {3},
      issn         = {1047-8477},
      address      = {San Diego, Calif.},
      publisher    = {Elsevier},
      reportid     = {FZJ-2014-05967},
      pages        = {249–258},
      year         = {2014},
      note         = {Article in press},
      abstract     = {Although PIN (PilT N-terminal)-domain proteins are known to
                      have ribonuclease activity, their specific mechanism of
                      action remains unknown. VapCs form a family of ribonucleases
                      that possess a PIN-domain assembly and are known as toxins.
                      The activities of VapCs are impaired by VapB antitoxins.
                      Here we present the crystal structure of the VapBC-15
                      toxin–antitoxin complex from Mycobacterium tuberculosis
                      determined to 2.1 Å resolution. The VapB-15 and VapC-15
                      components assemble into one heterotetramer (VapB2C2) and
                      two heterotrimers (VapBC2) in each asymmetric unit of the
                      crystal. The active site of VapC-15 toxin consists of a
                      cluster of acidic amino acid residues and two divalent metal
                      ions, forming a well organised ribonuclease active site. The
                      distribution of the catalytic-site residues of the VapC-15
                      toxin is similar to that of T4 RNase H and of Methanococcus
                      jannaschii FEN-1, providing strong evidence that these three
                      proteins share a similar mechanism of activity. The presence
                      of both VapB2C2 and VapBC2 emphasizes the fact that the same
                      antitoxin can bind the toxin in 1:1 and 1:2 ratios. The
                      crystal structure determination of the VapBC-15 complex
                      reveals for the first time a PIN-domain ribonuclease protein
                      that shows two metal ions at the active site and a variable
                      mode of toxin–antitoxin assembly. The structure further
                      shows that VapB-15 antitoxin binds to the same groove meant
                      for the binding of putative substrate (RNA), resulting in
                      the inhibition of VapC-15’s toxicity.},
      cin          = {ICS-6},
      ddc          = {540},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {452 - Structural Biology (POF2-452)},
      pid          = {G:(DE-HGF)POF2-452},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000346229500007},
      doi          = {10.1016/j.jsb.2014.10.002},
      url          = {https://juser.fz-juelich.de/record/172498},
}