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

Jimin Wang, James A. Hartling, John M. Flanagan

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Abstract

We have determined the crystal structure of the proteolytic component of the caseinolytic Clp protease (ClpP) from E. coli at 2.3 Å 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 ~51 Å in diameter. Access to the proteolytic chamber is controlled by two axial pores, each having a minimum diameter of ~10 Å. From the structural features of ClpP, we suggest a model for its action in degrading proteins.

Original languageEnglish (US)
Pages (from-to)447-456
Number of pages10
JournalCell
Volume91
Issue number4
DOIs
StatePublished - Nov 14 1997

All Science Journal Classification (ASJC) codes

  • Biochemistry, Genetics and Molecular Biology(all)

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