Clp Protease

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   Print3D 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 2 heptameric rings of ClpP 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. ADP binding site in Helicobacter pylori ClpX (PDB entry 1um8). 3D structures of Clp protease Clp protease 3D structures

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Michal Harel, Alexander Berchansky