Leitner A Joachimiak LA Bracher A Mönkemeyer L Walzthoeni T Chen B Pechmann S Holmes S Cong Y Ma B Ludtke S Chiu W Hartl FU Aebersold R Frydman J 2012 TRiC/CCT is a highly conserved and essential chaperonin that uses ATP cycling to facilitate folding of approximately 10% of the eukaryotic proteome. This 1 MDa hetero-oligomeric complex consists of two stacked rings of eight paralogous subunits each. Previously proposed TRiC models differ substantially in their subunit arrangements and ring register. Here, we integrate chemical crosslinking, mass spectrometry, and combinatorial modeling to reveal the definitive subunit arrangement of TRiC. In vivo disulfide mapping provided additional validation for the crosslinking-derived arrangement as the definitive TRiC topology. This subunit arrangement allowed the refinement of a structural model using existing X-ray diffraction data. The structure described here explains all available crosslink experiments, provides a rationale for previously unexplained structural features, and reveals a surprising asymmetry of charges within the chaperonin folding chamber. application/pdf https://sonar.ch/global/documents/265574 eng info:eu-repo/semantics/altIdentifier/doi/10.1016/j.str.2012.03.007 info:eu-repo/semantics/altIdentifier/pmid/22503819 info:eu-repo/semantics/openAccess Structure (London, England : 1993). - 2012 Animals Cattle Chaperonin Containing TCP-1 Eukaryota Models, Molecular Protein Conformation Protein Folding Protein Subunits Saccharomyces cerevisiae Tandem Mass Spectrometry X-Ray Diffraction The molecular architecture of the eukaryotic chaperonin TRiC/CCT. http://purl.org/coar/resource_type/c_6501