1TYF

THE STRUCTURE OF CLPP AT 2.3 ANGSTROM RESOLUTION SUGGESTS A MODEL FOR ATP-DEPENDENT PROTEOLYSIS

Summary for 1TYF

• Entry DOI: 10.2210/pdb1tyf/pdb
• Descriptor: CLP PEPTIDASE (2 entities in total)
• Functional Keywords: peptidase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P0A6G7
• Total number of polymer chains: 14
• Total formula weight: 302216.08

Authors

Wang, J.,Hartling, J.A.,Flanagan, J.M. (deposition date: 1997-10-13, release date: 1998-06-17, Last modification date: 2024-02-14)

Primary citation

Wang, J.,Hartling, J.A.,Flanagan, J.M.
The structure of ClpP at 2.3 A resolution suggests a model for ATP-dependent proteolysis.
Cell(Cambridge,Mass.), 91:447-456, 1997

PubMed Abstract: 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.

PubMed: 9390554
DOI: 10.1016/S0092-8674(00)80431-6

Experimental method

X-RAY DIFFRACTION (2.3 Å)