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@ARTICLE{Atkinson:858361,
      author       = {Atkinson, Sarah C. and Dogovski, Con and Wood, Kathleen and
                      Griffin, Michael D. W. and Gorman, Michael A. and Hor,
                      Lilian and Reboul, Cyril F. and Buckle, Ashley M. and
                      Wuttke, Joachim and Parker, Michael W. and Dobson, Renwick
                      C. J. and Perugini, Matthew A.},
      title        = {{S}ubstrate {L}ocking {P}romotes {D}imer-{D}imer {D}ocking
                      of an {E}nzyme {A}ntibiotic {T}arget},
      journal      = {Structure},
      volume       = {26},
      number       = {7},
      issn         = {0969-2126},
      address      = {Cambridge, Mass.},
      publisher    = {Cell Press},
      reportid     = {FZJ-2018-07248},
      pages        = {948 - 959.e5},
      year         = {2018},
      abstract     = {Protein dynamics manifested through structural flex-ibility
                      play a central role in the function of biologicalmolecules.
                      Here we explore the substrate-mediatedchange in protein
                      flexibility of an antibiotic targetenzyme, Clostridium
                      botulinum dihydrodipicolinatesynthase. We demonstrate that
                      the substrate, pyru-vate, stabilizes the more active
                      dimer-of-dimers ortetrameric form. Surprisingly, there is
                      little differencebetween the crystal structures of apo and
                      substrate-bound enzyme, suggesting protein dynamics may
                      beimportant. Neutron and small-angle X-ray
                      scatteringexperiments were used to probe
                      substrate-induceddynamics on the sub-second timescale, but
                      nosignificant changes were observed. We thereforedeveloped a
                      simple technique, coined protein dy-namics-mass spectrometry
                      (ProD-MS), which en-ables measurement of time-dependent
                      alkylation ofcysteine residues. ProD-MS together with
                      X-raycrystallography and analytical
                      ultracentrifugationanalyses indicates that pyruvate locks
                      the conforma-tion of the dimer that promotes docking to the
                      moreactive tetrameric form, offering insight into
                      ligand-mediated stabilization of multimeric enzymes.},
      cin          = {JCNS-FRM-II},
      ddc          = {540},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218},
      pnm          = {6G15 - FRM II / MLZ (POF3-6G15) / 6G4 - Jülich Centre for
                      Neutron Research (JCNS) (POF3-623)},
      pid          = {G:(DE-HGF)POF3-6G15 / G:(DE-HGF)POF3-6G4},
      experiment   = {EXP:(DE-MLZ)SPHERES-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:29804823},
      UT           = {WOS:000437809100005},
      doi          = {10.1016/j.str.2018.04.014},
      url          = {https://juser.fz-juelich.de/record/858361},
}