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@ARTICLE{Creon:634789,
      author       = {Creon, Anne and Scheer, Theresa Emilie Sophie and Reinke,
                      Patrick and Rahmani Mashhour, Aida and Günther, Sebastian
                      and Niebling, Stephan and Schamoni-Kast, Kira and Uetrecht,
                      Charlotte and Meents, Alke and Chapman, Henry N. and
                      Sprenger, Janina and Lane, Thomas},
      title        = {{S}tatistical crystallography reveals an allosteric network
                      in {SARS}-{C}o{V}-2 {M} pro},
      reportid     = {PUBDB-2025-02613},
      year         = {2025},
      abstract     = {To interpret and transmit biological signals, proteins use
                      correlated motions. Experimental determination of these
                      dynamics with atomic resolution remains a key challenge.
                      Here, using thousands of crystals of the main protease
                      (Mpro) from SARS-CoV-2, we were able to infer a model of the
                      protein’s correlated motions. Mpro is regulated by
                      concentration, becoming enzymatically active after forming a
                      homodimer. To understand the correlated motions that enable
                      dimerization to activate catalysis, we employed our model,
                      predicting which regions of the dimerization domain are
                      structurally linked to the active site. Mutations at these
                      positions, expected to disrupt catalysis, resulted in a
                      dramatic reduction in activity in one case, a mild effect in
                      the second, and none in the third. Additional
                      crystallography and biophysical experiments provide a
                      mechanistic explanation for these results. Our work suggests
                      that a statistical crystallography can determine protein
                      correlated motions and rationalize their biological
                      function.},
      cin          = {CFEL-I / FS-CFEL-1-BMX / DOOR ; HAS-User},
      cid          = {I:(DE-H253)CFEL-I-20161114 /
                      I:(DE-H253)FS-CFEL-1-BMX-20210408 /
                      I:(DE-H253)HAS-User-20120731},
      pnm          = {633 - Life Sciences – Building Blocks of Life: Structure
                      and Function (POF4-633) / 6G3 - PETRA III (DESY) (POF4-6G3)
                      / AIM, DFG project G:(GEPRIS)390715994 - EXC 2056: CUI:
                      Advanced Imaging of Matter (390715994) / 05K19GU4 - SFX2:
                      Hochdurchsatz Serielle-Femtosekunden Kristallographie @ EU
                      XFEL. (BMBF-05K19GU4) / InternLabs-0011 - HIR3X - Helmholtz
                      International Laboratory on Reliability, Repetition, Results
                      at the most advanced X-ray Sources $(2020_InternLabs-0011)$
                      / ARIADNE - Redefining mass spectrometry – a breakthrough
                      platform for real-time noninvasive breath analysis with
                      single ion detection of intact viruses and bacteria and
                      post-analysis molecular characterization (964553) / SPOCkS
                      MS - Sampling Protein cOmplex Conformational Space with
                      native top down Mass Spectrometry (759661)},
      pid          = {G:(DE-HGF)POF4-633 / G:(DE-HGF)POF4-6G3 /
                      G:(GEPRIS)390715994 / G:(DE-Ds200)BMBF-05K19GU4 /
                      $G:(DE-HGF)2020_InternLabs-0011$ / G:(EU-Grant)964553 /
                      G:(EU-Grant)759661},
      experiment   = {EXP:(DE-H253)P-P11-20150101},
      typ          = {PUB:(DE-HGF)25},
      doi          = {10.1101/2025.01.28.635305},
      url          = {https://bib-pubdb1.desy.de/record/634789},
}