[HTML][HTML] Human mitochondrial ClpP is a stable heptamer that assembles into a tetradecamer in the presence of ClpX
SG Kang, MN Dimitrova, J Ortega, A Ginsburg… - Journal of Biological …, 2005 - ASBMB
The functional form of ClpP, the proteolytic component of ATP-dependent Clp proteases, is a
hollow-cored particle composed of two heptameric rings joined face-to-face forming an
aqueous chamber containing the proteolytic active sites. We have found that isolated human
mitochondrial ClpP (hClpP) is stable as a heptamer and remains a monodisperse species (s
20, w 7.0 S; M app 169, 200) at concentrations≥ 3 mg/ml. Heptameric hClpP has no
proteolytic activity and very low peptidase activity. In the presence of ATP, hClpX interacts …
hollow-cored particle composed of two heptameric rings joined face-to-face forming an
aqueous chamber containing the proteolytic active sites. We have found that isolated human
mitochondrial ClpP (hClpP) is stable as a heptamer and remains a monodisperse species (s
20, w 7.0 S; M app 169, 200) at concentrations≥ 3 mg/ml. Heptameric hClpP has no
proteolytic activity and very low peptidase activity. In the presence of ATP, hClpX interacts …