Ontology highlight
ABSTRACT:
SUBMITTER: Bewley MC
PROVIDER: S-EPMC3433037 | biostudies-literature | 2009 Feb
REPOSITORIES: biostudies-literature
Bewley Maria C MC Graziano Vito V Griffin Kathleen K Flanagan John M JM
Journal of structural biology 20081111 2
Clp is a barrel-shaped hetero-oligomeric ATP-dependent protease comprising a hexameric ATPase (ClpX or ClpA) that unfolds protein substrates and translocates them into the central chamber of the tetradecameric proteolytic component (ClpP) where they are degraded processively to short peptides. Chamber access is controlled by the N-terminal 20 residues (for Escherichia coli) in ClpP that prevent entry of large polypeptides in the absence of the ATPase subunits and ATP hydrolysis. Remarkably, remo ...[more]