Clp Protease

Function Clp protease (CLP) is a serine peptidase which hydrolyzes proteins in the presence of ATP and Mg+2 ion. CLP is found in mitochondria. CLP participates in degradation of misfolded proteins. For more details see Clp protease Zinc Fingers Molecular Playground/ClpP Molecular Playground/E. coli ClpP. Structural highlights CLP is a heterodimer containing an ATP-binding regulatory subunit A ClpA or Hsp100 in Heat Shock Proteins and catalytic subunit P ClpP. The proteolytic complex is composed of flanked by hexameric rings of ClpA. For full proteolytic activity ClpP must associate with one of two related ATPase subunits: ClpA and ClpX. 3D structures of Clp protease Clp protease 3D structures

spinqualitylabelsall models E. coli Clp protease catalytic subunit (PDB entry 1tyf) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image