Crystallography and mutagenesis point to an essential role for the N-terminus of human mitochondrial ClpP.

@article{Kang2004CrystallographyAM,
  title={Crystallography and mutagenesis point to an essential role for the N-terminus of human mitochondrial ClpP.},
  author={Sung Gyun Kang and Michael R. Maurizi and Mark Thompson and Timothy C. Mueser and Bijan Ahvazi},
  journal={Journal of structural biology},
  year={2004},
  volume={148 3},
  pages={338-52}
}
We have determined a 2.1 A crystal structure for human mitochondrial ClpP (hClpP), the proteolytic component of the ATP-dependent ClpXP protease. HClpP has a structure similar to that of the bacterial enzyme, with the proteolytic active sites sequestered within an aqueous chamber formed by face-to-face assembly of the two heptameric rings. The hydrophobic N-terminal peptides of the subunits are bound within the narrow (12 A) axial channel, positioned to interact with unfolded substrates… CONTINUE READING

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