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@ARTICLE{Docquier:95357,
      author       = {Docquier, J. D. and Calderone, V. and De Luca, F. and
                      Benvenuti, M. and Giuliani, F. and Bellucci, L. and Tafi, A.
                      and Nordmann, P. and Botta, M. and Rossolini, G. M. and
                      Mangani, S. and DESY},
      title        = {{C}rystal structure of the {OXA}-48 beta-lactamase reveals
                      mechanistic diversity among class {D} carbapenemases.},
      journal      = {Chemistry $\&$ biology},
      volume       = {16},
      issn         = {1074-5521},
      address      = {Amsterdam [u.a.]},
      publisher    = {Cell Press},
      reportid     = {PHPPUBDB-20354},
      pages        = {540-547},
      year         = {2009},
      note         = {(c) Elsevier Ltd; Open Archive},
      abstract     = {Carbapenem-hydrolyzing class D beta-lactamases (CHDLs) are
                      enzymes found in important Gram-negative pathogens (mainly
                      Acinetobacter baumannii and Enterobacteriaceae) that confer
                      resistance to beta-lactam antibiotics, and notably
                      carbapenems. The crystal structure of the OXA-48
                      carbapenemase was determined at pH 7.5 and at a resolution
                      of 1.9 A. Surprisingly, and by contrast with OXA-24, the
                      only other CHDL of known crystal structure, the structure of
                      OXA-48 was similar to OXA-10, an enzyme devoid of
                      carbapenemase activity, indicating that the hydrolysis of
                      these compounds could depend on subtle changes in the active
                      site region. Moreover, the active site groove of OXA-48 was
                      different from that of OXA-24 in shape, dimensions, and
                      charge distribution. Molecular dynamics pointed to the
                      functional relevance of residues located in or close to the
                      beta5-beta6 loop and allowed us to propose a mechanism for
                      carbapenem hydrolysis by OXA-48.},
      keywords     = {Bacterial Proteins: chemistry / Bacterial Proteins:
                      classification / Catalytic Domain / Computer Simulation /
                      Crystallography, X-Ray / Kinetics / Protein Structure,
                      Quaternary / beta-Lactamases: chemistry / beta-Lactamases:
                      classification / Bacterial Proteins (NLM Chemicals) /
                      beta-Lactamases (NLM Chemicals) / carbapenemase (NLM
                      Chemicals)},
      cin          = {EMBL(-2012)},
      ddc          = {540},
      cid          = {$I:(DE-H253)EMBL_-2012_-20130307$},
      pnm          = {DORIS Beamline BW7 (POF1-550)},
      pid          = {G:(DE-H253)POF1-BW7-20130405},
      experiment   = {EXP:(DE-H253)D-BW7-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:19477418},
      UT           = {WOS:000266620800009},
      doi          = {10.1016/j.chembiol.2009.04.010},
      url          = {https://bib-pubdb1.desy.de/record/95357},
}