Ontology highlight
ABSTRACT:
SUBMITTER: Wendler P
PROVIDER: S-EPMC2689388 | biostudies-literature | 2009 Apr
REPOSITORIES: biostudies-literature
Wendler Petra P Shorter James J Snead David D Plisson Celia C Clare Daniel K DK Lindquist Susan S Saibil Helen R HR
Molecular cell 20090401 1
The protein-remodeling machine Hsp104 dissolves amorphous aggregates as well as ordered amyloid assemblies such as yeast prions. Force generation originates from a tandem AAA+ (ATPases associated with various cellular activities) cassette, but the mechanism and allostery of this action remain to be established. Our cryoelectron microscopy maps of Hsp104 hexamers reveal substantial domain movements upon ATP binding and hydrolysis in the first nucleotide-binding domain (NBD1). Fitting atomic model ...[more]