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@ARTICLE{Reinke:593910,
      author       = {Reinke, Patrick and Schubert, Robin and Oberthür, Dominik
                      and Galchenkova, Marina and Rahmani Mashhour, Aida and
                      Guenther, Sebastian and Chretien, Anaïs and Round, Adam and
                      Seychell, Brandon Charles and Norton-Baker, Brenna and Kim,
                      Chan and Schmidt, Christina and Koua, Faisal H. M. and
                      Tolstikova, Alexandra and Ewert, Wiebke and Pena Murillo,
                      Gisel Esperanza and Mills, Grant and Kirkwood, Henry and
                      Brognaro, Hévila and Han, Huijong and Koliyadu, Jayanath
                      and Schulz, Joachim and Bielecki, Johan and Lieske, Julia
                      and Maracke, Julia and Knoska, Juraj and Lorenzen, Kristina
                      and Brings, Lea and Sikorski, Marcin and Kloos, Marco and
                      Vakili, Mohammad and Vagovic, Patrik and Middendorf, Philipp
                      and de Wijn, Raphael and Bean, Richard and Letrun, Romain
                      and Han, Seonghyun and Falke, Sven and Geng, Tian and Sato,
                      Tokushi and Srinivasan, Vasundara and Kim, Yoonhee and
                      Yefanov, Oleksandr M. and Gelisio, Luca and Beck, Tobias and
                      Doré, Andrew S. and Mancuso, Adrian P. and Betzel,
                      Christian and Bajt, Saša and Redecke, Lars and Chapman,
                      Henry N. and Meents, Alke and Turk, Dušan and Hinrichs,
                      Winfried and Lane, Thomas},
      title        = {{SARS}-{C}o{V}-2 {M}pro responds to oxidation by forming
                      disulfide and {NOS}/{SONOS} bonds},
      journal      = {Nature Communications},
      volume       = {15},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Nature Publishing Group UK},
      reportid     = {PUBDB-2023-05575},
      pages        = {3827},
      year         = {2024},
      abstract     = {The main protease (M$^{pro}$) of SARS-CoV-2 is critical for
                      viral function and a key drug target. Mpro is only active
                      when reduced; turnover ceases upon oxidation but is restored
                      by re-reduction. This suggests the system has evolved to
                      survive periods in an oxidative environment, but the
                      mechanism of this protection has not been confirmed. Here,
                      we report a crystal structure of oxidized M$^{pro}$ showing
                      a disulfide bond between the active site cysteine, C145, and
                      a distal cysteine, C117. Previous work proposed this
                      disulfide provides the mechanism of protection from
                      irreversible oxidation. M$^{pro}$ forms an obligate
                      homodimer, and the C117-C145 structure shows disruption of
                      interactions bridging the dimer interface, implying a
                      correlation between oxidation and dimerization. We confirm
                      dimer stability is weakened in solution upon oxidation.
                      Finally, we observe the protein’s crystallization behavior
                      is linked to its redox state. Oxidized M$^{pro}$
                      spontaneously forms a distinct, more loosely packed lattice.
                      Seeding with crystals of this lattice yields a structure
                      with an oxidation pattern incorporating one
                      cysteine-lysine-cysteine (SONOS) and two lysine-cysteine
                      (NOS) bridges. These structures further our understanding of
                      the oxidative regulation of M$^{pro}$ and the
                      crystallization conditions necessary to study this
                      structurally.},
      cin          = {CFEL-I / FS-CFEL-1-PBIO / FS-CFEL-1-BMX /
                      $XFEL_E1_SPB/SFX$},
      ddc          = {500},
      cid          = {I:(DE-H253)CFEL-I-20161114 /
                      I:(DE-H253)FS-CFEL-1-PBIO-20210408 /
                      I:(DE-H253)FS-CFEL-1-BMX-20210408 /
                      $I:(DE-H253)XFEL_E1_SPB_SFX-20210408$},
      pnm          = {633 - Life Sciences – Building Blocks of Life: Structure
                      and Function (POF4-633) / 6G3 - PETRA III (DESY) (POF4-6G3)
                      / InternLabs-0011 - HIR3X - Helmholtz International
                      Laboratory on Reliability, Repetition, Results at the most
                      advanced X-ray Sources $(2020_InternLabs-0011)$ / FISCOV -
                      FISCOV Helmholtz large research infrastructures in the fight
                      against epidemic outbreaks (FISCOV) / DFG project
                      G:(GEPRIS)390715994 - EXC 2056: CUI: Advanced Imaging of
                      Matter (390715994) / DFG project G:(GEPRIS)194651731 - EXC
                      1074: Hamburger Zentrum für ultraschnelle Beobachtung
                      (CUI): Struktur, Dynamik und Kontrolle von Materie auf
                      atomarer Skala (194651731)},
      pid          = {G:(DE-HGF)POF4-633 / G:(DE-HGF)POF4-6G3 /
                      $G:(DE-HGF)2020_InternLabs-0011$ / G:(DE-HGF)FISCOV /
                      G:(GEPRIS)390715994 / G:(GEPRIS)194651731},
      experiment   = {EXP:(DE-H253)P-P11-20150101 /
                      EXP:(DE-H253)XFEL-SPB-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:38714735},
      UT           = {WOS:001215774800049},
      doi          = {10.1038/s41467-024-48109-3},
      url          = {https://bib-pubdb1.desy.de/record/593910},
}