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@ARTICLE{Inoue:16351,
      author       = {Inoue, R. and Biehl, R. and Rosenkranz, T. and Fitter, J.
                      and Monkenbusch, M. and Radulescu, A. and Farago, B. and
                      Richter, D.},
      title        = {{L}arge domain fluctuations on 50ns timescale enable
                      catalytic activity in phoshpglycerate kinase},
      journal      = {Biophysical journal},
      volume       = {99},
      number       = {7},
      issn         = {0006-3495},
      address      = {New York, NY},
      publisher    = {Rockefeller Univ. Press},
      reportid     = {PreJuSER-16351},
      pages        = {2309 - 2317},
      year         = {2010},
      note         = {T.R. acknowledges financial support by the International
                      Helmholtz Research School on Biophysics and Soft Matter
                      (BioSoft).},
      abstract     = {Large-scale domain motions of enzymes are often essential
                      for their biological function. Phosphoglycerate kinase has a
                      wide open domain structure with a hinge near the active
                      center between the two domains. Applying neutron spin echo
                      spectroscopy and small-angle neutron scattering we have
                      investigated the internal domain dynamics. Structural
                      analysis reveals that the holoprotein in solution seems to
                      be more compact compared to the crystal structure but would
                      not allow the functionally important phosphoryl transfer
                      between the substrates if the protein were static. Brownian
                      large-scale domain fluctuation dynamics on a timescale of 50
                      ns was revealed by neutron spin echo spectroscopy. The
                      dynamics observed was compared to the displacement patterns
                      of low-frequency normal modes. The displacements along the
                      normal-mode coordinates describe our experimental results
                      reasonably well. In particular, the domain movements
                      facilitate a close encounter of the key residues in the
                      active center to build the active configuration. The
                      observed dynamics shows that the protein has the flexibility
                      to allow fluctuations and displacements that seem to enable
                      the function of the protein. Moreover, the presence of the
                      substrates increases the rigidity, which is deduced from a
                      faster dynamics with smaller amplitude.},
      keywords     = {Biocatalysis / Diffusion / Kinetics / Models, Molecular /
                      Neutron Diffraction / Phosphoglycerate Kinase: chemistry /
                      Phosphoglycerate Kinase: metabolism / Protein Structure,
                      Secondary / Protein Structure, Tertiary / Saccharomyces
                      cerevisiae: enzymology / Scattering, Small Angle /
                      Structure-Activity Relationship / Time Factors /
                      Phosphoglycerate Kinase (NLM Chemicals) / J (WoSType)},
      cin          = {ICS-1 / JCNS-1 / JCNS (München) ; Jülich Centre for
                      Neutron Science JCNS (München) ; JCNS-FRM-II / ICS-5},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-1-20110106 / I:(DE-Juel1)JCNS-1-20110106 /
                      I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)ICS-5-20110106},
      pnm          = {BioSoft: Makromolekulare Systeme und biologische
                      Informationsverarbeitung / Großgeräte für die Forschung
                      mit Photonen, Neutronen und Ionen (PNI)},
      pid          = {G:(DE-Juel1)FUEK505 / G:(DE-Juel1)FUEK415},
      experiment   = {EXP:(DE-MLZ)KWS1-20140101},
      shelfmark    = {Biophysics},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:20923666},
      pmc          = {pmc:PMC3042550},
      UT           = {WOS:000282850600037},
      doi          = {10.1016/j.bpj.2010.08.017},
      url          = {https://juser.fz-juelich.de/record/16351},
}