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

  title={ClpP: a structurally dynamic protease regulated by AAA+ proteins.},
  author={John A Alexopoulos and Alba Guarn{\'e} and Joaquin Ortega},
  journal={Journal of structural biology},
  volume={179 2},
Proteolysis is an important process for many aspects of bacterial physiology. Clp proteases carry out a large proportion of protein degradation in bacteria. These enzymes assemble in complexes that combine the protease ClpP and the unfoldase, ClpA or ClpX. ClpP oligomerizes as two stacked heptameric rings enclosing a central chamber containing the proteolytic sites. ClpX and ClpA assemble into hexameric rings that bind both axial surfaces of the ClpP tetradecamer forming a barrel-like complex… CONTINUE READING


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Structural insights into the conformational diversity of ClpP from Bacillus subtilis

  • B. G. Lee, E. Y. Park, K. E. Lee, H. Jeon, K. H. Sung
  • Mol . Cells
  • 2011
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