A tetrahedral transition state at the active sites of the 20S proteasome is coupled to opening of the alpha-ring channel.

@article{Osmulski2009ATT,
  title={A tetrahedral transition state at the active sites of the 20S proteasome is coupled to opening of the alpha-ring channel.},
  author={Pawel A. Osmulski and Mark Hochstrasser and Maria E. Gaczynska},
  journal={Structure},
  year={2009},
  volume={17 8},
  pages={
          1137-47
        }
}
Intrinsic conformational transitions contribute to the catalytic action of many enzymes. Here we use a single-molecule approach to demonstrate how such transitions are linked to the catalytic sites of the eukaryotic proteasome, an essential protease of the ubiquitin pathway. The active sites of the cylindrical proteasomal core particle are located in a central chamber accessible through gated entry channels. By using atomic force microscopy, we found continual alternation between open and… CONTINUE READING

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