Staggered ATP binding mechanism of eukaryotic chaperonin TRiC (CCT) revealed through high-resolution cryo-EM

@article{Zang2016StaggeredAB,
  title={Staggered ATP binding mechanism of eukaryotic chaperonin TRiC (CCT) revealed through high-resolution cryo-EM},
  author={Yun-xiang Zang and M. Jin and Huping Wang and Zhicheng Cui and Liangliang Kong and Caixuan Liu and Yao Cong},
  journal={Nature Structural \&Molecular Biology},
  year={2016},
  volume={23},
  pages={1083-1091}
}
The eukaryotic chaperonin TRiC (or CCT) assists in the folding of 10% of cytosolic proteins. Here we present two cryo-EM structures of Saccharomyces cerevisiae TRiC in a newly identified nucleotide partially preloaded (NPP) state and in the ATP-bound state, at 4.7-Å and 4.6-Å resolution, respectively. Through inner-subunit eGFP tagging, we identified the subunit locations in open-state TRiC and found that the CCT2 subunit pair forms an unexpected Z shape. ATP binding induces a dramatic… Expand
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