The structures of exocyst subunit Exo70p and the Exo84p C-terminal domains reveal a common motif

@article{Dong2005TheSO,
  title={The structures of exocyst subunit Exo70p and the Exo84p C-terminal domains reveal a common motif},
  author={Gang Dong and Alex H. Hutagalung and Chunmei Fu and Peter J. Novick and Karin M Reinisch},
  journal={Nature Structural &Molecular Biology},
  year={2005},
  volume={12},
  pages={1094-1100}
}
The exocyst is a large complex that is required for tethering vesicles at the final stages of the exocytic pathway in all eukaryotes. Here we present the structures of the Exo70p subunit of this complex and of the C-terminal domains of Exo84p, at 2.0-Å and 2.85-Å resolution, respectively. Exo70p forms a 160-Å-long rod with a novel fold composed of contiguous α-helical bundles. The Exo84p C terminus also forms a long rod (80 Å), which unexpectedly has the same fold as the Exo70p N terminus. Our… CONTINUE READING
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