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
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 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.
3D structures of Clp protease
Clp protease 3D structures
