Ontology highlight
ABSTRACT:
SUBMITTER: Stinson BM
PROVIDER: S-EPMC4424054 | biostudies-literature | 2015 May
REPOSITORIES: biostudies-literature
Nature structural & molecular biology 20150413 5
The hexameric AAA+ ring of Escherichia coli ClpX, an ATP-dependent machine for protein unfolding and translocation, functions with the ClpP peptidase to degrade target substrates. For efficient function, ClpX subunits must switch between nucleotide-loadable (L) and nucleotide-unloadable (U) conformations, but the roles of switching are uncertain. Moreover, it is controversial whether working AAA+-ring enzymes assume symmetric or asymmetric conformations. Here, we show that a covalent ClpX ring w ...[more]