[HTML][HTML] Functional proteolytic complexes of the human mitochondrial ATP-dependent protease, hClpXP
SG Kang, J Ortega, SK Singh, N Wang, N Huang… - Journal of Biological …, 2002 - ASBMB
Human mitochondrial ClpP (hClpP) and ClpX (hClpX) were separately cloned, and the
expressed proteins were purified. Electron microscopy confirmed that hClpP forms
heptameric rings and that hClpX forms a hexameric ring. Complexes of a double heptameric
ring of hClpP with hexameric hClpX rings bound on each side are stable in the presence of
ATP or adenosine 5′-(3-thiotriphosphate)(ATPγS), indicating that a symmetry mismatch is a
universal feature of Clp proteases. hClpXP displays both ATP-dependent proteolytic activity …
expressed proteins were purified. Electron microscopy confirmed that hClpP forms
heptameric rings and that hClpX forms a hexameric ring. Complexes of a double heptameric
ring of hClpP with hexameric hClpX rings bound on each side are stable in the presence of
ATP or adenosine 5′-(3-thiotriphosphate)(ATPγS), indicating that a symmetry mismatch is a
universal feature of Clp proteases. hClpXP displays both ATP-dependent proteolytic activity …