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@ARTICLE{Gabba:171792,
      author       = {Gabba, Matteo and Poblete, Simon and Rosenkranz, T. and
                      Katranidis, Alexandros and Kempe, D. and Züchner, Tina and
                      Winkler, Roland G. and Gompper, Gerhard and Fitter, Jörg},
      title        = {{C}onformational state distributions and catalytically
                      relevant dynamics of a hinge-bending enzyme studied by
                      single-molecule {FRET} and a coarse-grained simulation},
      journal      = {Biophysical journal},
      volume       = {107},
      number       = {8},
      issn         = {0006-3495},
      publisher    = {Elsevier Inc.},
      reportid     = {FZJ-2014-05354},
      pages        = {1913-1923},
      year         = {2014},
      abstract     = {Over the last few decades, a view has emerged showing that
                      multidomain enzymes are biological machines evolved to
                      harness stochastic kicks of solvent particles into highly
                      directional functional motions. These intrinsic motions are
                      structurally encoded, and Nature makes use of them to
                      catalyze chemical reactions by means of ligand-induced
                      conformational changes and states redistribution. Such
                      mechanisms align reactive groups for efficient chemistry and
                      stabilize conformers most proficient for catalysis. By
                      combining single-molecule Förster resonance energy transfer
                      measurements with normal mode analysis and coarse-grained
                      mesoscopic simulations, we obtained results for a
                      hinge-bending enzyme, namely phosphoglycerate kinase (PGK),
                      which support and extend these ideas. From single-molecule
                      Förster resonance energy transfer, we obtained insight into
                      the distribution of conformational states and the dynamical
                      properties of the domains. The simulations allowed for the
                      characterization of interdomain motions of a compact state
                      of PGK. The data show that PGK is intrinsically a highly
                      dynamic system sampling a wealth of conformations on
                      timescales ranging from nanoseconds to milliseconds and
                      above. Functional motions encoded in the fold are performed
                      by the PGK domains already in its ligand-free form, and
                      substrate binding is not required to enable them. Compared
                      to other multidomain proteins, these motions are rather fast
                      and presumably not rate-limiting in the enzymatic reaction.
                      Ligand binding slightly readjusts the orientation of the
                      domains and feasibly locks the protein motions along a
                      preferential direction. In addition, the functionally
                      relevant compact state is stabilized by the substrates, and
                      acts as a prestate to reach active conformations by means of
                      Brownian motions.},
      cin          = {ICS-5 / IAS-2 / ICS-2},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-5-20110106 / I:(DE-Juel1)IAS-2-20090406 /
                      I:(DE-Juel1)ICS-2-20110106},
      pnm          = {452 - Structural Biology (POF2-452) / 451 - Soft Matter
                      Composites (POF2-451)},
      pid          = {G:(DE-HGF)POF2-452 / G:(DE-HGF)POF2-451},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000343682700017},
      pubmed       = {pmid:25418172},
      doi          = {10.1016/j.bpj.2014.08.016},
      url          = {https://juser.fz-juelich.de/record/171792},
}