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@ARTICLE{Barabas:166788,
      author       = {Barabas, O. and Nemeth, V. and Bodor, A. and Perczel, A.
                      and Rosta, E. and Kele, Z. and Zagyva, I. and Szabadka, Z.
                      and Grolmusz, V. I. and Wilmanns, M. and Vertessy, B. G.},
      title        = {{C}atalytic mechanism of  -phosphate attack in d{UTP}ase
                      is revealed by {X}-ray crystallographic snapshots of
                      distinct intermediates, 31{P}-{NMR} spectroscopy and
                      reaction path modelling},
      journal      = {Nucleic acids symposium series},
      volume       = {41},
      number       = {22},
      issn         = {1362-4962},
      address      = {Oxford},
      publisher    = {Oxford Univ. Press8619},
      reportid     = {DESY-2014-01622},
      pages        = {10542 - 10555},
      year         = {2013},
      abstract     = {Enzymatic synthesis and hydrolysis of nucleoside phosphate
                      compounds play a key role in various biological pathways,
                      like signal transduction, DNA synthesis and metabolism.
                      Although these processes have been studied extensively,
                      numerous key issues regarding the chemical pathway and
                      atomic movements remain open for many enzymatic reactions.
                      Here, using the Mason-Pfizer monkey retrovirus dUTPase, we
                      study the dUTPase-catalyzed hydrolysis of dUTP, an incorrect
                      DNA building block, to elaborate the mechanistic details at
                      high resolution. Combining mass spectrometry analysis of the
                      dUTPase-catalyzed reaction carried out in and quantum
                      mechanics/molecular mechanics (QM/MM) simulation, we show
                      that the nucleophilic attack occurs at the α-phosphate
                      site. Phosphorus-31 NMR spectroscopy ((31)P-NMR) analysis
                      confirms the site of attack and shows the capability of
                      dUTPase to cleave the dUTP analogue α,β-imido-dUTP,
                      containing the imido linkage usually regarded to be
                      non-hydrolyzable. We present numerous X-ray crystal
                      structures of distinct dUTPase and nucleoside phosphate
                      complexes, which report on the progress of the chemical
                      reaction along the reaction coordinate. The presently used
                      combination of diverse structural methods reveals details of
                      the nucleophilic attack and identifies a novel
                      enzyme-product complex structure.},
      cin          = {EMBL},
      ddc          = {540},
      cid          = {I:(DE-H253)EMBL-20120731},
      pnm          = {DORIS Beamline BW7 (POF2-54G13) / DORIS Beamline K1.1
                      (POF2-54G13) / DORIS Beamline K1.3 (POF2-54G13)},
      pid          = {G:(DE-H253)POF2-BW7-20130405 /
                      G:(DE-H253)POF2-K1.1-20130405 /
                      G:(DE-H253)POF2-K1.3-20130405},
      experiment   = {EXP:(DE-H253)D-BW7-20150101 / EXP:(DE-H253)D-K1.1-20150101
                      / EXP:(DE-H253)D-K1.3-20150101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000329874400050},
      pubmed       = {pmid:23982515},
      doi          = {10.1093/nar/gkt756},
      url          = {https://bib-pubdb1.desy.de/record/166788},
}