The ClpP N-terminus coordinates substrate access with protease active site reactivity.

@article{Jennings2008TheCN,
  title={The ClpP N-terminus coordinates substrate access with protease active site reactivity.},
  author={Laura D. Jennings and Jen Bohon and Mark R. Chance and Stuart Licht},
  journal={Biochemistry},
  year={2008},
  volume={47 42},
  pages={11031-40}
}
Energy-dependent protein degradation machines, such as the Escherichia coli protease ClpAP, require regulated interactions between the ATPase component (ClpA) and the protease component (ClpP) for function. Recent studies indicate that the ClpP N-terminus is essential in these interactions, yet the dynamics of this region remain unclear. Here, we use synchrotron hydroxyl radical footprinting and kinetic studies to characterize functionally important conformational changes of the ClpP N-terminus… CONTINUE READING