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@ARTICLE{Balaev:299285,
      author       = {Balaev, Vladislav and Lashkov, Aleksandr and Gabdulkhakov,
                      Azat and Dontsova, M. V. and Mironov, A. S. and Betzel, C.
                      and Mikhailov, A. M.},
      title        = {{T}hree-dimensional structures of unligated uridine
                      phosphorylase from {Y}ersinia pseudotuberculosis at 1.4 Å
                      resolution and its complex with an antibacterial drug},
      journal      = {Crystallography reports},
      volume       = {60},
      number       = {4},
      issn         = {1562-689X},
      address      = {Woodbury, NY},
      publisher    = {MAIK "Nauka/Interperiodica"},
      reportid     = {PUBDB-2016-01942},
      pages        = {525 - 531},
      year         = {2015},
      note         = {(c) Pleiades Publishing, Inc. Post referee full text in
                      progress.},
      abstract     = {Uridine phosphorylases play an essential role in the
                      cellular metabolism of some antibacterial agents. Acute
                      infectious diseases (bubonic plague, yersiniosis,
                      pseudotuberculosis, etc., caused by bacteria of the genus
                      Yersinia) are treated using both sulfanilamide medicines and
                      antibiotics, including trimethoprim. The action of an
                      antibiotic on a bacterial cell is determined primarily by
                      the character of its interactions with cellular components,
                      including those which are not targets (for example, with
                      pyrimidine phosphorylases). This type of interaction should
                      be taken into account in designing drugs. The
                      three-dimensional structure of uridine phosphorylase from
                      the bacterium Yersinia pseudotuberculosis (YptUPh) with the
                      free active site was determined for the first time by X-ray
                      crystallography and refined at 1.40 Å resolution (DPI =
                      0.062 Å; IDPDB: 4OF4). The structure of the complex of Ypt
                      UPh with the bacteriostatic drug trimethoprim was studied by
                      molecular docking and molecular dynamics methods. The
                      trimethoprim molecule was shown to be buffered by the enzyme
                      Ypt UPh, resulting in a decrease in the efficiency of the
                      treatment of infectious diseases caused by bacteria of the
                      genus Yersinia with trimethoprim.},
      cin          = {DOOR / X-RAY},
      ddc          = {540},
      cid          = {I:(DE-H253)HAS-User-20120731 / I:(DE-H253)X-RAY-20120731},
      pnm          = {6G3 - PETRA III (POF3-622)},
      pid          = {G:(DE-HGF)POF3-6G3},
      experiment   = {EXP:(DE-H253)P-P11-20150101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000358644700010},
      doi          = {10.1134/S1063774515040069},
      url          = {https://bib-pubdb1.desy.de/record/299285},
}