{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Sauer RT"],"funding":["NIDDK NIH HHS","Howard Hughes Medical Institute","NIAID NIH HHS","NIH","NIGMS NIH HHS"],"pagination":["188-204"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9871882"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["57(2)"],"pubmed_abstract":["ClpXP is an archetypical AAA+ protease, consisting of ClpX and ClpP. ClpX is an ATP-dependent protein unfoldase and polypeptide translocase, whereas ClpP is a self-compartmentalized peptidase. ClpXP is currently the only AAA+ protease for which high-resolution structures exist, the molecular basis of recognition for a protein substrate is understood, extensive biochemical and genetic analysis have been performed, and single-molecule optical trapping has allowed direct visualization of the kinetics of substrate unfolding and translocation. In this review, we discuss our current understanding of ClpXP structure and function, evaluate competing sequential and probabilistic mechanisms of ATP hydrolysis, and highlight open questions for future exploration."],"journal":["Critical reviews in biochemistry and molecular biology"],"pubmed_title":["Structure and function of ClpXP, a AAA+ proteolytic machine powered by probabilistic ATP hydrolysis."],"pmcid":["PMC9871882"],"funding_grant_id":["5R01-DK115558","R35 GM141517","T32 GM007287","RO1-AI016892","R01 DK115558","R37 AI015706","RO1-GM101988","R35-GM141517","R01 GM101988","5T32-GM007287","R01 AI016892"],"pubmed_authors":["Baker TA","Bell TA","Sauer RT","Fei X"],"additional_accession":[]},"is_claimable":false,"name":"Structure and function of ClpXP, a AAA+ proteolytic machine powered by probabilistic ATP hydrolysis.","description":"ClpXP is an archetypical AAA+ protease, consisting of ClpX and ClpP. ClpX is an ATP-dependent protein unfoldase and polypeptide translocase, whereas ClpP is a self-compartmentalized peptidase. ClpXP is currently the only AAA+ protease for which high-resolution structures exist, the molecular basis of recognition for a protein substrate is understood, extensive biochemical and genetic analysis have been performed, and single-molecule optical trapping has allowed direct visualization of the kinetics of substrate unfolding and translocation. In this review, we discuss our current understanding of ClpXP structure and function, evaluate competing sequential and probabilistic mechanisms of ATP hydrolysis, and highlight open questions for future exploration.","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Apr","modification":"2025-04-26T13:19:40.865Z","creation":"2025-04-06T14:10:53.296Z"},"accession":"S-EPMC9871882","cross_references":{"pubmed":["34923891"],"doi":["10.1080/10409238.2021.1979461"]}}