Crystal structure at 1.9A of E. coli ClpP with a peptide covalently bound at the active site.

@article{Szyk2006CrystalSA,
  title={Crystal structure at 1.9A of E. coli ClpP with a peptide covalently bound at the active site.},
  author={Agnieszka Szyk and Michael Robert Maurizi},
  journal={Journal of structural biology},
  year={2006},
  volume={156 1},
  pages={
          165-74
        }
}
ClpP, the proteolytic component of the ATP-dependent ClpAP and ClpXP chaperone/protease complexes, has 14 identical subunits organized in two stacked heptameric rings. The active sites are in an interior aqueous chamber accessible through axial channels. We have determined a 1.9 A crystal structure of Escherichia coli ClpP with benzyloxycarbonyl-leucyltyrosine chloromethyl ketone (Z-LY-CMK) bound at each active site. The complex mimics a tetrahedral intermediate during peptide cleavage, with… CONTINUE READING
BETA

Citations

Publications citing this paper.
SHOWING 1-10 OF 39 CITATIONS

ClpP: a structurally dynamic protease regulated by AAA+ proteins.

  • Journal of structural biology
  • 2012
VIEW 5 EXCERPTS
CITES BACKGROUND
HIGHLY INFLUENCED

Crystal structure of a bacterial signal Peptide peptidase.

  • Journal of molecular biology
  • 2008
VIEW 3 EXCERPTS
CITES BACKGROUND & METHODS
HIGHLY INFLUENCED

Similar Papers

Loading similar papers…