title: ClpXP, an ATP-powered unfolding and protein-degradation machine.
abstract: ClpXP is a AAA+ protease that uses the energy of ATP binding and hydrolysis to perform mechanical work during targeted protein degradation within cells. ClpXP consists of hexamers of a AAA+ ATPase (ClpX) and a tetradecameric peptidase (ClpP). Asymmetric ClpX hexamers bind unstructured peptide tags in protein substrates, unfold stable tertiary structure in the substrate, and then translocate the unfolded polypeptide chain into an internal proteolytic compartment in ClpP. Here, we review our present understanding of ClpXP structure and function, as revealed by two decades of biochemical and biophysical studies.
authors: Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
authors: Tania A
authors: TA
authors: Baker
authors: Robert T
authors: RT
authors: Sauer
mesh_terms: D000255:Adenosine Triphosphate / Q000737:chemistry*; D020816:Amino Acid Motifs; D020134:Catalytic Domain; D049071:Endopeptidase Clp / Q000737:chemistry*; D029968:Escherichia coli Proteins / Q000737:chemistry*; D006801:Humans; D006868:Hydrolysis; D011485:Protein Binding; D054730:Protein Interaction Domains and Motifs; D020836:Protein Structure, Quaternary; D058767:Protein Unfolding; D059748:Proteolysis
chemical_list: D029968:Escherichia coli Proteins; D000255:Adenosine Triphosphate; C483573:ClpXP protease, E coli; D049071:Endopeptidase Clp