Ontology highlight
ABSTRACT:
SUBMITTER: Stinson BM
PROVIDER: S-EPMC3674332 | biostudies-literature | 2013 Apr
REPOSITORIES: biostudies-literature
Stinson Benjamin M BM Nager Andrew R AR Glynn Steven E SE Schmitz Karl R KR Baker Tania A TA Sauer Robert T RT
Cell 20130401 3
ClpX, a AAA+ ring homohexamer, uses the energy of ATP binding and hydrolysis to power conformational changes that unfold and translocate target proteins into the ClpP peptidase for degradation. In multiple crystal structures, some ClpX subunits adopt nucleotide-loadable conformations, others adopt unloadable conformations, and each conformational class exhibits substantial variability. Using mutagenesis of individual subunits in covalently tethered hexamers together with fluorescence methods to ...[more]