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. ClpX or ATP-dependent Clp protease ATP-binding subunit ClpX is a molecular chaperone which alters the shape of DNA during bacteriophage μ transposition. For details see Molecular Playground/Hexameric ClpX 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 or ATP-binding Clp protease ATP-binding subunit ClpX. in Helicobacter pylori ClpX (PDB entry 1um8). 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