报告题目：Visualization of the Eukaryotic Chaperonin TRiC/CCT and the 24-meric Enzymatic Active Hemocyanin by cryo-EM
报告人：Yao Cong Ph. D.
National Center for Macromolecular Imaging, Baylor College of Medicine, Houston, TX, USA
时 间：2009年7月30日（周四）下午 3：00
主 持 人：朱 平 研究员
Defects in protein folding lead to many human diseases such as Alzheimer’s, Huntington’s, or Mad Cow’s disease. Chaperones can serve to prevent protein misfolding and aggregation in the cell. The eukaryotic chaperonin TRiC/CCT folds ~10% of cytosolic proteins including many key structural and regulatory proteins, many of which cannot be folded by any other chaperone. TRiC assistant substrate folding is an ATP-driven process. Utilizing cryo-EM single particle analysis in combination with comparative modeling and flexible fitting, my study provides the first comprehensive structural mechanism of TRiC conformational changes in the ATPase cycle. In addition, I will present a high-resolution asymmetric structure of TRiC in the closed state without any symmetry imposed in the 3D reconstruction. This study reveals the nucleotide binding strength variation among different subunits of TRiC, and the special arrangement of the 8 distinct subunits of TRiC.