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@ARTICLE{Freischem:902419,
      author       = {Freischem, Stefan and Grimm, Immanuel and López-Pérez,
                      Arancha and Willbold, Dieter and Klenke, Burkhard and Vuong,
                      Cuong and Dingley, Andrew J. and Weiergräber, Oliver H.},
      title        = {{I}nteraction {M}ode of the {N}ovel {M}onobactam {AIC}499
                      {T}argeting {P}enicillin {B}inding {P}rotein 3 of
                      {G}ram-{N}egative {B}acteria},
      journal      = {Biomolecules},
      volume       = {11},
      number       = {7},
      issn         = {2218-273X},
      address      = {Basel},
      publisher    = {MDPI},
      reportid     = {FZJ-2021-04241},
      pages        = {1057 -},
      year         = {2021},
      abstract     = {Novel antimicrobial strategies are urgently required
                      because of the rising threat of multi drug resistant
                      bacterial strains and the infections caused by them. Among
                      the available target structures, the so-called penicillin
                      binding proteins are of particular interest, owing to their
                      good accessibility in the periplasmic space, and the lack of
                      homologous proteins in humans, reducing the risk of side
                      effects of potential drugs. In this report, we focus on the
                      interaction of the innovative β-lactam antibiotic AIC499
                      with penicillin binding protein 3 (PBP3) from Escherichia
                      coli and Pseudomonas aeruginosa. This recently developed
                      monobactam displays broad antimicrobial activity, against
                      Gram-negative strains, and improved resistance to most
                      classes of β-lactamases. By analyzing crystal structures of
                      the respective complexes, we were able to explore the
                      binding mode of AIC499 to its target proteins. In addition,
                      the apo structures determined for PBP3, from P. aeruginosa
                      and the catalytic transpeptidase domain of the E. coli
                      orthologue, provide new insights into the dynamics of these
                      proteins and the impact of drug binding.},
      cin          = {IBI-7},
      ddc          = {570},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551) /
                      5241 - Molecular Information Processing in Cellular Systems
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF3-551 / G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:34356681},
      UT           = {WOS:000676509400001},
      doi          = {10.3390/biom11071057},
      url          = {https://juser.fz-juelich.de/record/902419},
}