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]
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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.
