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@ARTICLE{Leysen:142547,
      author       = {Leysen, S. and Vanderkelen, L. and Weeks, S. D. and
                      Michiels, C. W. and Strelkov, S. V. and DESY},
      title        = {{S}tructural basis of bacterial defense against g-type
                      lysozyme-based innate immunity},
      journal      = {Cellular and molecular life sciences},
      volume       = {70},
      issn         = {1420-682X},
      address      = {Basel},
      publisher    = {Birkhäuser},
      reportid     = {PHPPUBDB-25506},
      pages        = {1-10},
      year         = {2013},
      note         = {© Springer Basel; Post referee fulltext in progress;
                      Embargo 12 months from publication},
      abstract     = {Gram-negative bacteria can produce specific proteinaceous
                      inhibitors to defend themselves against the lytic action of
                      host lysozymes. So far, four different lysozyme inhibitor
                      families have been identified. Here, we report the crystal
                      structure of the Escherichia coli periplasmic lysozyme
                      inhibitor of g-type lysozyme (PliG-Ec) in complex with
                      Atlantic salmon g-type lysozyme (SalG) at a resolution of
                      0.95 Å, which is exceptionally high for a complex of two
                      proteins. The structure reveals for the first time the
                      mechanism of g-type lysozyme inhibition by the PliG family.
                      The latter contains two specific conserved regions that are
                      essential for its inhibitory activity. The inhibitory
                      complex formation is based on a double 'key-lock' mechanism.
                      The first key-lock element is formed by the insertion of two
                      conserved PliG regions into the active site of the lysozyme.
                      The second element is defined by a distinct pocket of PliG
                      accommodating a lysozyme loop. Computational analysis
                      indicates that this pocket represents a suitable site for
                      small molecule binding, which opens an avenue for the
                      development of novel antibacterial agents that suppress the
                      inhibitory activity of PliG.},
      keywords     = {Animals / Crystallography / Escherichia coli: chemistry /
                      Escherichia coli: immunology / Escherichia coli Proteins:
                      chemistry / Escherichia coli Proteins: metabolism /
                      Immunity, Innate: immunology / Models, Molecular /
                      Muramidase: chemistry / Muramidase: metabolism / Protein
                      Conformation / Salmo salar / Escherichia coli Proteins (NLM
                      Chemicals) / PliG protein, E coli (NLM Chemicals) /
                      Muramidase (NLM Chemicals)},
      cin          = {EMBL(-2012)},
      ddc          = {570},
      cid          = {$I:(DE-H253)EMBL_-2012_-20130307$},
      pnm          = {DORIS Beamline D1.2 (POF2-54G13)},
      pid          = {G:(DE-H253)POF2-D1.2-20130405},
      experiment   = {EXP:(DE-H253)D-D1.2-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:23086131},
      UT           = {WOS:000315343600011},
      doi          = {10.1007/s00018-012-1184-1},
      url          = {https://bib-pubdb1.desy.de/record/142547},
}