Ontology highlight
ABSTRACT:
SUBMITTER: Glynn SE
PROVIDER: S-EPMC3372766 | biostudies-literature | 2012 May
REPOSITORIES: biostudies-literature
Glynn Steven E SE Nager Andrew R AR Baker Tania A TA Sauer Robert T RT
Nature structural & molecular biology 20120506 6
In the Escherichia coli ClpXP protease, a hexameric ClpX ring couples ATP binding and hydrolysis to mechanical protein unfolding and translocation into the ClpP degradation chamber. Rigid-body packing between the small AAA+ domain of each ClpX subunit and the large AAA+ domain of its neighbor stabilizes the hexamer. By connecting the parts of each rigid-body unit with disulfide bonds or linkers, we created covalently closed rings that retained robust activity. A single-residue insertion in the h ...[more]