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@ARTICLE{Kalisman:139206,
      author       = {Kalisman, N. and Schröder, Gunnar and Levitt, M.},
      title        = {{T}he {C}rystal {S}tructures of the {E}ukaryotic
                      {C}haperonin {CCT} {R}eveal {I}ts {F}unctional
                      {P}artitioning},
      journal      = {Structure},
      volume       = {21},
      number       = {4},
      issn         = {0969-2126},
      address      = {London [u.a.]},
      publisher    = {Elsevier Science},
      reportid     = {FZJ-2013-05209},
      pages        = {540-549},
      year         = {2013},
      abstract     = {In eukaryotes, CCT is essential for the correct and
                      efficient folding of many cytosolic proteins, most notably
                      actin and tubulin. Structural studies of CCT have been
                      hindered by the failure of standard crystallographic
                      analysis to resolve its eight different subunit types at low
                      resolutions. Here, we exhaustively assess the R value fit of
                      all possible CCT models to available crystallographic data
                      of the closed and open forms with resolutions of 3.8 Å and
                      5.5 Å, respectively. This unbiased analysis finds the
                      native subunit arrangements with overwhelming significance.
                      The resulting structures provide independent
                      crystallographic proof of the subunit arrangement of CCT and
                      map major asymmetrical features of the particle onto
                      specific subunits. The actin and tubulin substrates both
                      bind around subunit CCT6, which shows other structural
                      anomalies. CCT is thus clearly partitioned, both
                      functionally and evolutionary, into a substrate-binding side
                      that is opposite to the ATP-hydrolyzing side.},
      cin          = {ICS-6},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {452 - Structural Biology (POF2-452)},
      pid          = {G:(DE-HGF)POF2-452},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000317800100004},
      pubmed       = {pmid:23478063},
      doi          = {10.1016/j.str.2013.01.017},
      url          = {https://juser.fz-juelich.de/record/139206},
}