Ontology highlight
ABSTRACT:
SUBMITTER: Mazal H
PROVIDER: S-EPMC6440998 | biostudies-literature | 2019 Mar
REPOSITORIES: biostudies-literature
Mazal Hisham H Iljina Marija M Barak Yoav Y Elad Nadav N Rosenzweig Rina R Goloubinoff Pierre P Riven Inbal I Haran Gilad G
Nature communications 20190329 1
Large protein machines are tightly regulated through allosteric communication channels. Here we demonstrate the involvement of ultrafast conformational dynamics in allosteric regulation of ClpB, a hexameric AAA+ machine that rescues aggregated proteins. Each subunit of ClpB contains a unique coiled-coil structure, the middle domain (M domain), proposed as a control element that binds the co-chaperone DnaK. Using single-molecule FRET spectroscopy, we probe the M domain during the chaperone cycle ...[more]