% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Gore:642342,
      author       = {Gore, Gargi and Prester, Andreas and von Stetten, David and
                      Bartels, Kim and Schulz, Eike C.},
      title        = {{B}inding mode of {I}soxazolyl {P}enicillins to a
                      {C}lass-{A} β-lactamase at ambient conditions},
      journal      = {Communications chemistry},
      volume       = {8},
      number       = {1},
      issn         = {2399-3669},
      address      = {[London]},
      publisher    = {Macmillan Publishers Limited, part of Springer Nature},
      reportid     = {PUBDB-2025-05497},
      pages        = {387},
      year         = {2025},
      abstract     = {The predominant resistance mechanism observed in
                      Gram-negative bacteria involves the production of
                      β-lactamases, which catalyse the hydrolysis of β-lactam
                      antibiotics, thereby rendering them ineffective. Although
                      Isoxazolyl Penicillins have been available since the 1970s,
                      there are currently no structures in complex with class-A
                      β-lactamases available. Here we have analysed the structure
                      of the clinically relevant β-lactamase CTX-M-14 from
                      Klebsiella pneumoniae near physiological temperatures, via
                      serial synchrotron crystallography. We demonstrate the
                      acyl-enzyme intermediates of the catalytically impaired
                      CTX-M-14 mutant E166A in complex with three
                      Isoxazolyl-Penicillins: Oxacillin, Cloxacillin and
                      Dicloxacillin. Structural comparisons of CTX-M-Penicillin
                      complexes show that, while conserved active-site
                      interactions are maintained, each Isoxazolyl-Penicillin
                      adopts a distinct conformation. While the three derivatives
                      differ only by one and two chlorine atoms, respectively,
                      their conformational heterogeneity appears to be increased
                      by chlorination of the phenyl ring.},
      cin          = {MPSD},
      ddc          = {540},
      cid          = {I:(DE-H253)MPSD-20120731},
      pnm          = {DFG project G:(GEPRIS)458246365 - Zeitaufgelöste
                      Strukturanalysde der extended spectrum Beta-Lactamase
                      CTX-M-14 (458246365) / 899 - ohne Topic (POF4-899)},
      pid          = {G:(GEPRIS)458246365 / G:(DE-HGF)POF4-899},
      experiment   = {EXP:(DE-MLZ)NOSPEC-20140101},
      typ          = {PUB:(DE-HGF)16},
      doi          = {10.1038/s42004-025-01801-x},
      url          = {https://bib-pubdb1.desy.de/record/642342},
}