Recent structural insights into the mechanism of ClpP protease regulation by AAA+ chaperones and small molecules.

ABSTRACT: ClpP is a highly conserved serine protease that is a critical enzyme in maintaining protein homeostasis and is an important drug target in pathogenic bacteria and various cancers. In its functional form, ClpP is a self-compartmentalizing protease composed of two stacked heptameric rings that allow protein degradation to occur within the catalytic chamber. ATPase chaperones such as ClpX and ClpA are hexameric ATPases that form larger complexes with ClpP and are responsible for the selection and unfolding of protein substrates prior to their degradation by ClpP. Although individual structures of ClpP and ATPase chaperones have offered mechanistic insights into their function and regulation, their structures together as a complex have only been recently determined to high resolution. Here, we

SUBMITTER: Mabanglo MF 

PROVIDER: S-EPMC9035409 | biostudies-literature | 2022 May

REPOSITORIES: biostudies-literature