The Molecular Architecture of the Eukaryotic Chaperonin TRiC/CCT
Autor: | Ruedi Aebersold, Wah Chiu, Susan Holmes, S. Ludtke, Leonie Mönkemeyer, Andreas Bracher, Lukasz A. Joachimiak, Yao Cong, Boxue Ma, Bryan Chen, F. Ulrich Hartl, Sebastian Pechmann, Judith Frydman, Thomas Walzthoeni, Alexander Leitner |
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Rok vydání: | 2012 |
Předmět: |
Models
Molecular Protein Folding Protein Conformation Protein subunit Saccharomyces cerevisiae macromolecular substances Article Chaperonin 03 medical and health sciences Protein structure X-Ray Diffraction Tandem Mass Spectrometry Structural Biology Animals Molecular Biology 030304 developmental biology 0303 health sciences biology 030302 biochemistry & molecular biology Disulfide bond Eukaryota biology.organism_classification Protein Subunits Crystallography Chaperone (protein) Proteome biology.protein Biophysics Cattle Protein folding sense organs Chaperonin Containing TCP-1 |
Zdroj: | Structure Structure; Vol 20 |
ISSN: | 0969-2126 |
Popis: | Summary 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. |
Databáze: | OpenAIRE |
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