Clp protease

spinqualitylabelsall models PDB ID 1tyf Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
1tyf, resolution 2.30Å ()
Activity:	Endopeptidase Clp, with EC number 3.4.21.92
Structural annotation: Resources: CATH : 1Tyfa00, 1Tyfb00, 1Tyfc00, 1Tyfd00, 1Tyfe00, 1Tyff00, 1Tyfg00, 1Tyfh00, 1Tyfi00, 1Tyfj00, 1Tyfk00, 1Tyfl00, 1Tyfm00, 1Tyfn00 InterPro : Ipr001907 Pfam : PF00574 SCOP : d1tyfa_, d1tyfb_, d1tyfc_, d1tyfd_, d1tyfe_, d1tyff_, d1tyfg_, d1tyfh_, d1tyfi_, d1tyfj_, d1tyfk_, d1tyfl_, d1tyfm_, d1tyfn_ UniProt : P0A6G7
Functional annotation: Cellular component: cytoplasm membrane fraction Biological process: response to stress proteolysis Molecular function: endopeptidase Clp activity serine-type endopeptidase activity peptidase activity hydrolase activity
Evolutionary conservation: Toggle Conservation Colors: Rows = identical sequences: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
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 PROTEOLYSISTHE STRUCTURE OF CLPP AT 2.3 ANGSTROM RESOLUTION SUGGESTS A MODEL FOR ATP-DEPENDENT PROTEOLYSIS

Publication Abstract from PubMed

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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.

About this StructureAbout this Structure

1TYF is a 14 chain structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

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Two pores are found on each end of the peptidase . In fact, one can even look view completely through the large lumen of the tetradecamer and out the other side of the structure

ReferenceReference

Created with the participation of Wayne Decatur.