Ontology highlight
ABSTRACT:
SUBMITTER: Douglas NR
PROVIDER: S-EPMC3055171 | biostudies-literature | 2011 Jan
REPOSITORIES: biostudies-literature
Douglas Nicholai R NR Reissmann Stefanie S Zhang Junjie J Chen Bo B Jakana Joanita J Kumar Ramya R Chiu Wah W Frydman Judith J
Cell 20110101 2
Group II chaperonins are ATP-dependent ring-shaped complexes that bind nonnative polypeptides and facilitate protein folding in archaea and eukaryotes. A built-in lid encapsulates substrate proteins within the central chaperonin chamber. Here, we describe the fate of the substrate during the nucleotide cycle of group II chaperonins. The chaperonin substrate-binding sites are exposed, and the lid is open in both the ATP-free and ATP-bound prehydrolysis states. ATP hydrolysis has a dual function i ...[more]