Clp protease
From Proteopedia
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| 1tyf, resolution 2.30Å (default scene) | |||||||||
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| Activity: | Endopeptidase Clp, with EC number 3.4.21.92 | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
THE STRUCTURE OF CLPP AT 2.3 ANGSTROM RESOLUTION SUGGESTS A MODEL FOR ATP-DEPENDENT PROTEOLYSIS
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.
The structure of ClpP at 2.3 A resolution suggests a model for ATP-dependent proteolysis., Wang J, Hartling JA, Flanagan JM, Cell. 1997 Nov 14;91(4):447-56. PMID:9390554
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
Two pores are found on each end of the peptidase which are obvious when all proteins atoms shown as spheres with Van der Waals radii. In fact, one can even look view completely through the large lumen of the tetradecamer and out the other side of the structure if the complex is centered on the pores and held still.
Reference
- Wang J, Hartling JA, Flanagan JM. The structure of ClpP at 2.3 A resolution suggests a model for ATP-dependent proteolysis. Cell. 1997 Nov 14;91(4):447-56. PMID:9390554
Created with the participation of Wayne Decatur.
