Ontology highlight
ABSTRACT:
SUBMITTER: Fei X
PROVIDER: S-EPMC4156775 | biostudies-literature | 2014 Sep
REPOSITORIES: biostudies-literature
Fei Xue X Ye Xiang X LaRonde Nicole A NA Lorimer George H GH
Proceedings of the National Academy of Sciences of the United States of America 20140818 35
The GroE chaperonins assist substrate protein (SP) folding by cycling through several conformational states. With each cycle the SP is, in turn, captured, unfolded, briefly encapsulated (t1/2 ∼ 1 s), and released by the chaperonin complex. The protein-folding functional form is the US-football-shaped GroEL:GroES2 complex. We report structures of two such "football" complexes to ∼ 3.7-Å resolution; one is empty whereas the other contains encapsulated SP in both chambers. Although encapsulated SP ...[more]