Ontology highlight
ABSTRACT:
SUBMITTER: Schmitz KR
PROVIDER: S-EPMC4217457 | biostudies-literature | 2014 Oct
REPOSITORIES: biostudies-literature
Schmitz Karl R KR Carney Daniel W DW Sello Jason K JK Sauer Robert T RT
Proceedings of the National Academy of Sciences of the United States of America 20140929 43
Caseinolytic peptidase P (ClpP), a double-ring peptidase with 14 subunits, collaborates with ATPases associated with diverse activities (AAA+) partners to execute ATP-dependent protein degradation. Although many ClpP enzymes self-assemble into catalytically active homo-tetradecamers able to cleave small peptides, the Mycobacterium tuberculosis enzyme consists of discrete ClpP1 and ClpP2 heptamers that require a AAA+ partner and protein-substrate delivery or a peptide agonist to stabilize assembl ...[more]