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@ARTICLE{Musiani:201310,
      author       = {Musiani, Francesco and Ippoliti, Emiliano and Micheletti,
                      Cristian and Carloni, Paolo and Ciurli, Stefano},
      title        = {{C}onformational {F}luctuations of {U}re{G}, an
                      {I}ntrinsically {D}isordered {E}nzyme},
      journal      = {Biochemistry},
      volume       = {52},
      number       = {17},
      issn         = {1520-4995},
      address      = {Columbus, Ohio},
      publisher    = {American Chemical Society},
      reportid     = {FZJ-2015-03615},
      pages        = {2949 - 2954},
      year         = {2013},
      abstract     = {UreG proteins are small GTP binding (G) proteins that
                      catalyze the hydrolysis of GTP necessary for the maturation
                      of urease, a virulence factor in bacterial pathogenesis.
                      UreG proteins are the first documented cases of
                      intrinsically disordered enzymes. The comprehension of the
                      dynamics of folding−unfolding events occurring in this
                      protein could shed light on the enzymatic mechanism of UreG.
                      Here, we used the recently developed replica exchange with
                      solute tempering (REST2) computational methodology to
                      explore the conformational space of UreG from Helicobacter
                      pylori (HpUreG) and to identify its structural fluctuations.
                      The same simulation and analysis protocol has been applied
                      to HypB from Methanocaldococcus jannaschii (MjHypB), which
                      is closely related to UreG in both sequence and function,
                      even though it is not intrinsically disordered. A comparison
                      of the two systems reveals that both HpUreG and MjHypB
                      feature a substantial rigidity of the protein regions
                      involved in catalysis, justifying its residual catalytic
                      activity. On the other hand, HpUreG tends to unfold more
                      than MjHypB in portions involved in protein−protein
                      interactions with metallochaperones necessary for the
                      formation of multiprotein complexes known to be involved in
                      urease activation.},
      cin          = {GRS / IAS-5},
      ddc          = {570},
      cid          = {I:(DE-Juel1)GRS-20100316 / I:(DE-Juel1)IAS-5-20120330},
      pnm          = {899 - ohne Topic (POF2-899)},
      pid          = {G:(DE-HGF)POF2-899},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000318333100010},
      doi          = {10.1021/bi4001744},
      url          = {https://juser.fz-juelich.de/record/201310},
}