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@ARTICLE{Bartolucci:138438,
      author       = {Bartolucci, C. and Lamba, D. and Grazulis, S. and Manakova,
                      E. and Heumann, H. and DESY},
      title        = {{C}rystal structure of wild-type chaperonin {G}ro{EL}},
      journal      = {Journal of molecular biology},
      volume       = {354},
      issn         = {0022-2836},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier},
      reportid     = {PHPPUBDB-24644},
      pages        = {940-51},
      year         = {2005},
      abstract     = {The 2.9A resolution crystal structure of apo wild-type
                      GroEL was determined for the first time and represents the
                      reference structure, facilitating the study of structural
                      and functional differences observed in GroEL variants. Until
                      now the crystal structure of the mutant Arg13Gly, Ala126Val
                      GroEL was used for this purpose. We show that, due to the
                      mutations as well as to the presence of a crystallographic
                      symmetry, the ring-ring interface was inaccurately
                      described. Analysis of the present structure allowed the
                      definition of structural elements at this interface,
                      essential for understanding the inter-ring allosteric signal
                      transmission. We also show unambiguously that there is no
                      ATP-induced 102 degrees rotation of the apical domain helix
                      I around its helical axis, as previously assumed in the
                      crystal structure of the (GroEL-KMgATP)(14) complex, and
                      analyze the apical domain movements. These results enabled
                      us to compare our structure with other GroEL crystal
                      structures already published, allowing us to suggest a new
                      route through which the allosteric signal for negative
                      cooperativity propagates within the molecule. The proposed
                      mechanism, supported by known mutagenesis data, underlines
                      the importance of the switching of salt bridges.},
      keywords     = {Adenosine Triphosphate: pharmacology / Allosteric
                      Regulation / Chaperonin 60: chemistry / Chaperonin 60:
                      genetics / Chaperonins: chemistry / Chaperonins: genetics /
                      Crystallography, X-Ray / Escherichia coli Proteins / Models,
                      Molecular / Molecular Structure / Mutation, Missense /
                      Protein Conformation: drug effects / Chaperonin 60 (NLM
                      Chemicals) / Escherichia coli Proteins (NLM Chemicals) /
                      Adenosine Triphosphate (NLM Chemicals) / Chaperonins (NLM
                      Chemicals)},
      cin          = {HASYLAB / EMBL},
      ddc          = {570},
      cid          = {$I:(DE-H253)HASYLAB_-2012_-20130307$ /
                      $I:(DE-H253)EMBL_-2012_-20130307$},
      pnm          = {DORIS Beamline BW6 (POF1-550)},
      pid          = {G:(DE-H253)POF1-BW6-20130405},
      experiment   = {EXP:(DE-H253)D-BW6-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:16288915},
      UT           = {WOS:000234089600017},
      doi          = {10.1016/j.jmb.2005.09.096},
      url          = {https://bib-pubdb1.desy.de/record/138438},
}