Cryo-EM Structures of the Hsp104 Protein Disaggregase Captured in the ATP Conformation.

ABSTRACT: Hsp104 is a ring-forming, ATP-driven molecular machine that recovers functional protein from both stress-denatured and amyloid-forming aggregates. Although Hsp104 shares a common architecture with Clp/Hsp100 protein unfoldases, different and seemingly conflicting 3D structures have been reported. Examining the structure of Hsp104 poses considerable challenges because Hsp104 readily hydrolyzes ATP, whereas ATP analogs can be slowly turned over and are often contaminated with other nucleotide species. Here, we present the single-particle electron cryo-microscopy (cryo-EM) structures of a catalytically inactive Hsp104 variant (Hsp104_DWB) in the ATP-bound state determined between 7.7 Å and 9.3 Å resolution. Surprisingly, we observe that the Hsp104_DWB hexamer adopts distin

SUBMITTER: Lee S 

PROVIDER: S-EPMC6347426 | biostudies-literature | 2019 Jan

REPOSITORIES: biostudies-literature