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.^[1]
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.^[2] 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).^[3]

3D structures of Clp protease

Clp protease 3D structures