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@ARTICLE{AlvesFrana:606914,
      author       = {Alves França, Bruno and Falke, Sven and Rohde, Holger and
                      Betzel, Christian},
      title        = {{M}olecular insights into the dynamic modulation of
                      bacterial {C}lp{P} function and oligomerization by
                      peptidomimetic boronate compounds},
      journal      = {Scientific reports},
      volume       = {14},
      number       = {1},
      issn         = {2045-2322},
      address      = {[London]},
      publisher    = {Macmillan Publishers Limited, part of Springer Nature},
      reportid     = {PUBDB-2024-01690},
      pages        = {2572},
      year         = {2024},
      abstract     = {Bacterial caseinolytic protease P subunit (ClpP) is
                      important and vital for cell survival and infectivity.
                      Recent publications describe and discuss the complex
                      structure–function relationship of ClpP and its processive
                      activity mediated by 14 catalytic sites. Even so, there are
                      several aspects yet to be further elucidated, such as the
                      paradoxical allosteric modulation of ClpP by peptidomimetic
                      boronates. These compounds bind to all catalytic sites, and
                      in specific conditions, they stimulate a dysregulated
                      degradation of peptides and globular proteins, instead of
                      inhibiting the enzymatic activity, as expected for serine
                      proteases in general. Aiming to explore and explain this
                      paradoxical effect, we solved and refined the crystal
                      structure of native ClpP from Staphylococcus epidermidis
                      (Se), an opportunistic pathogen involved in nosocomial
                      infections, as well as ClpP in complex with ixazomib at 1.90
                      Å and 2.33 Å resolution, respectively. The interpretation
                      of the crystal structures, in combination with complementary
                      biochemical and biophysical data, shed light on how ixazomib
                      affects the ClpP conformational state and activity.
                      Moreover, SEC-SAXS and DLS measurements show, for the first
                      time, that a peptidomimetic boronate compound also induces
                      the assembly of the tetradecameric structure from isolated
                      homomeric heptameric rings of a gram-positive organism.},
      cin          = {FS-CFEL-1-BMX / FS-PS / EMBL-User},
      ddc          = {600},
      cid          = {I:(DE-H253)FS-CFEL-1-BMX-20210408 /
                      I:(DE-H253)FS-PS-20131107 / I:(DE-H253)EMBL-User-20120814},
      pnm          = {633 - Life Sciences – Building Blocks of Life: Structure
                      and Function (POF4-633) / 6G3 - PETRA III (DESY) (POF4-6G3)},
      pid          = {G:(DE-HGF)POF4-633 / G:(DE-HGF)POF4-6G3},
      experiment   = {EXP:(DE-H253)P-P12-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:38296985},
      UT           = {WOS:001155680400031},
      doi          = {10.1038/s41598-024-51787-0},
      url          = {https://bib-pubdb1.desy.de/record/606914},
}