% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Das:207477,
      author       = {Das, Uddipan and Pogenberg, Vivian and Subhramanyam, Udaya
                      Kumar Tiruttani and Wilmanns, Matthias and Gourinath,
                      Samudrala and Srinivasan, Alagiri},
      title        = {{C}rystal {S}tructure of the {V}ap{BC}-15 {C}omplex from
                      {M}ycobacterium {T}uberculosis {R}eveals a {T}wo-{M}etal
                      {I}on dependent {PIN}-{D}omain {R}ibonuclease and a
                      {V}ariable {M}ode of {T}oxin-{A}ntitoxin {A}ssemblypetea},
      journal      = {Journal of structural biology},
      volume       = {188},
      number       = {3},
      issn         = {1047-8477},
      address      = {San Diego, Calif.},
      publisher    = {Elsevier},
      reportid     = {PUBDB-2015-01365},
      pages        = {249 - 258},
      year         = {2014},
      note         = {(c) Elsevier Inc. Post referee full text in progress.
                      Embargo for full text 1 year from 22. Oct. 2014.},
      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 (VapB$_2$C$_2$)
                      and two heterotrimers (VapBC$_2$) 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 VapB$_2$C$_2$ and VapBC$_2$ 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          = {EMBL},
      ddc          = {540},
      cid          = {I:(DE-H253)EMBL-20120731},
      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:000346229500007},
      pubmed       = {pmid:25450593},
      doi          = {10.1016/j.jsb.2014.10.002},
      url          = {https://bib-pubdb1.desy.de/record/207477},
}