4V94

Molecular architecture of the eukaryotic chaperonin TRiC/CCT derived by a combination of chemical crosslinking and mass-spectrometry, XL-MS

This is a non-PDB format compatible entry.

Summary for 4V94

• Entry DOI: 10.2210/pdb4v94/pdb
• Descriptor: T-complex protein 1 subunit zeta, ADENOSINE-5'-DIPHOSPHATE, BERYLLIUM TRIFLUORIDE ION, ... (11 entities in total)
• Functional Keywords: chaperonin, nano cage, protein folding, molecular chaperone, atpase, cytosol, chaperone
• Biological source: Saccharomyces cerevisiae (Baker's yeast); More
• Cellular location: Cytoplasm: P39079 P47079 P42943 P40413 P39076 P39078 P12612 P39077
• Total number of polymer chains: 32
• Total formula weight: 1952737.22

Authors

Leitner, A.,Joachimiak, L.A.,Bracher, A.,Walzthoeni, T.,Chen, B.,Monkemeyer, L.,Pechmann, S.,Holmes, S.,Cong, Y.,Ma, B.,Ludtke, S.,Chiu, W.,Hartl, F.U.,Aebersold, R.,Frydman, J. (deposition date: 2012-01-11, release date: 2014-07-09, Last modification date: 2024-02-28)

Primary citation

Leitner, A.,Joachimiak, L.A.,Bracher, A.,Monkemeyer, L.,Walzthoeni, T.,Chen, B.,Pechmann, S.,Holmes, S.,Cong, Y.,Ma, B.,Ludtke, S.,Chiu, W.,Hartl, F.U.,Aebersold, R.,Frydman, J.
The Molecular Architecture of the Eukaryotic Chaperonin TRiC/CCT.
Structure, 20:814-825, 2012

PubMed Abstract: 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.

PubMed: 22503819
DOI: 10.1016/j.str.2012.03.007

Experimental method

X-RAY DIFFRACTION (3.8 Å)