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@ARTICLE{Samygina:81600,
      author       = {Samygina, V. R. and Moiseev, V. M. and Rodina, E. V. and
                      Vorobyeva, N. N. and Popov, A. N. and Kurilova, S. A. and
                      Nazarova, T. I. and Avaeva, S. M. and Bartunik, H. D. and
                      DESY},
      title        = {{R}eversible inhibition of {E}scherichia coli inorganic
                      pyrophosphatase by fluoride: trapped catalytic intermediates
                      in cryo-crystallographic studies},
      journal      = {Journal of molecular biology},
      volume       = {366},
      issn         = {0022-2836},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier},
      reportid     = {PHPPUBDB-6428},
      pages        = {1305-1317},
      year         = {2007},
      abstract     = {Here, we describe high-resolution X-ray structures of
                      Escherichia coli inorganic pyrophosphatase (E-PPase)
                      complexed with the substrate, magnesium, or manganese
                      pyrophosphate. The structures correspond to steps in the
                      catalytic synthesis of enzyme-bound pyrophosphate (PP(i)) in
                      the presence of fluoride as an inhibitor of hydrolysis. The
                      catalytic reaction intermediates were trapped applying a new
                      method that we developed for initiating hydrolytic activity
                      in the E-PPase crystal. X-ray structures were obtained for
                      three consecutive states of the enzyme in the course of
                      hydrolysis. Comparative analysis of these structures showed
                      that the Mn2+-supported hydrolysis of the phosphoanhydride
                      bond is followed by a fast release of the leaving phosphate
                      from the P1 site. The electrophilic phosphate P2 is trapped
                      in the "down" conformation. Its movement into the "up"
                      position most likely represents the rate-limiting step of
                      Mn2+-supported hydrolysis. We further determined the crystal
                      structure of the Arg43Gln mutant variant of E-PPase
                      complexed with one phosphate and four Mn ions.},
      keywords     = {Binding Sites / Catalysis / Diphosphates: chemistry /
                      Diphosphates: pharmacology / Enzyme Activation / Escherichia
                      coli: enzymology / Fluorides: chemistry / Fluorides:
                      pharmacology / Hydrogen-Ion Concentration / Hydrolysis /
                      Inorganic Pyrophosphatase: chemistry / Inorganic
                      Pyrophosphatase: genetics / Inorganic Pyrophosphatase:
                      metabolism / Magnesium: chemistry / Magnesium: pharmacology
                      / Manganese: chemistry / Manganese: pharmacology / Models,
                      Molecular / Mutation / Protein Isoforms / Substrate
                      Specificity / X-Ray Diffraction: methods / Diphosphates (NLM
                      Chemicals) / Fluorides (NLM Chemicals) / Protein Isoforms
                      (NLM Chemicals) / Magnesium (NLM Chemicals) / Manganese (NLM
                      Chemicals) / Inorganic Pyrophosphatase (NLM Chemicals)},
      cin          = {MPG},
      ddc          = {570},
      cid          = {$I:(DE-H253)MPG_-2012_-20120307$},
      pnm          = {DORIS Beamline BW6 (POF1-550)},
      pid          = {G:(DE-H253)POF1-BW6-20130405},
      experiment   = {EXP:(DE-H253)D-BW6-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:17196979},
      UT           = {WOS:000244649500021},
      doi          = {10.1016/j.jmb.2006.11.082},
      url          = {https://bib-pubdb1.desy.de/record/81600},
}