The structure of ClpP at 2.3 A resolution suggests a model for ATP-dependent proteolysis

Cell. 1997 Nov 14;91(4):447-56. doi: 10.1016/s0092-8674(00)80431-6.


We have determined the crystal structure of the proteolytic component of the caseinolytic Clp protease (ClpP) from E. coli at 2.3 A resolution using an ab initio phasing procedure that exploits the internal 14-fold symmetry of the oligomer. The structure of a ClpP monomer has a distinct fold that defines a fifth structural family of serine proteases but a conserved catalytic apparatus. The active protease resembles a hollow, solid-walled cylinder composed of two 7-fold symmetric rings stacked back-to-back. Its 14 proteolytic active sites are located within a central, roughly spherical chamber approximately 51 A in diameter. Access to the proteolytic chamber is controlled by two axial pores, each having a minimum diameter of approximately 10 A. From the structural features of ClpP, we suggest a model for its action in degrading proteins.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenosine Triphosphatases*
  • Adenosine Triphosphate / metabolism*
  • Amino Acid Sequence
  • Binding Sites
  • Crystallography, X-Ray
  • Endopeptidase Clp
  • Escherichia coli / enzymology
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Conformation*
  • Protein Folding
  • Proteins / metabolism*
  • Serine Endopeptidases / chemistry*
  • Serine Endopeptidases / metabolism
  • Surface Properties


  • Proteins
  • Adenosine Triphosphate
  • Serine Endopeptidases
  • Endopeptidase Clp
  • Adenosine Triphosphatases

Associated data

  • PDB/1TFY