Ontology highlight
ABSTRACT:
SUBMITTER: Koike-Takeshita A
PROVIDER: S-EPMC4208008 | biostudies-literature | 2014 Oct
REPOSITORIES: biostudies-literature
The Journal of biological chemistry 20140908 43
The Escherichia coli chaperonin GroEL is a double-ring chaperone that assists protein folding with the aid of GroES and ATP. Asp-398 in GroEL is known as one of the critical residues on ATP hydrolysis because GroEL(D398A) mutant is deficient in ATP hydrolysis (<2% of the wild type) but not in ATP binding. In the archaeal Group II chaperonin, another aspartate residue, Asp-52 in the corresponding E. coli GroEL, in addition to Asp-398 is also important for ATP hydrolysis. We investigated the role ...[more]