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@ARTICLE{Knospe:638191,
      author       = {Knospe, C. Vivien and Ortiz, Julio and Reiners, Jens and
                      Kedrov, Alexej and Gertzen, Christoph G. W. and Smits,
                      Sander H. J. and Schmitt, Lutz},
      title        = {{S}tructural insights into the substrate binding mechanism
                      of the class {I} dehydratase {M}ad{B}},
      journal      = {Communications biology},
      volume       = {8},
      number       = {1},
      issn         = {2399-3642},
      address      = {London},
      publisher    = {Springer Nature},
      reportid     = {PUBDB-2025-04009},
      pages        = {1032},
      year         = {2025},
      abstract     = {In the battle against antimicrobial resistance,
                      lantibiotics have emerged as promising new sources for
                      antimicrobial drugs. Their exceptional stability is due to
                      characteristic modifications termed (methyl-)lanthionine
                      rings. Genome mining efforts have identified hundreds of
                      lantibiotics by detecting gene operons, so-called
                      biosynthetic gene clusters (BGC), which encode cysteine-rich
                      peptides (30-50 amino acids in size) and enzymes responsible
                      for dehydration and cyclization, catalyzing the
                      post-translational ring formation. One such identified,
                      class I lantibiotic is maddinglicin from Clostridium
                      maddingley. Here, we present single particle cryo-EM
                      structures of the dehydratase MadB in both, its apo-state
                      and in complex with a leader peptide of maddinglicin,
                      revealing a distinct conformational change upon substrate
                      binding. Small-angle X-ray scattering studies elucidate the
                      substrate binding site for the C-terminal part of
                      maddinglicin. Furthermore, a substrate specificity analysis
                      was performed highlighting a critical stretch of amino acids
                      within the maddinglicin leader sequence that is crucial for
                      binding. Here, we provide molecular insights into the
                      conformational changes, principles of substrate recognition
                      and ligand:protein stoichiometry of a class I lantibiotic
                      dehydratase.},
      cin          = {EMBL-User},
      ddc          = {570},
      cid          = {I:(DE-H253)EMBL-User-20120814},
      pnm          = {6G3 - PETRA III (DESY) (POF4-6G3)},
      pid          = {G:(DE-HGF)POF4-6G3},
      experiment   = {EXP:(DE-H253)P-P12-20150101},
      typ          = {PUB:(DE-HGF)16},
      doi          = {10.1038/s42003-025-08454-5},
      url          = {https://bib-pubdb1.desy.de/record/638191},
}