6N8Z

HSP104DWB extended conformation

6N8Z の概要

• エントリーDOI: 10.2210/pdb6n8z/pdb
• 関連するPDBエントリー: 6n8t 6n8v
• EMDBエントリー: 0375 0376 0377
• 分子名称: Heat shock protein 104, ADENOSINE-5'-TRIPHOSPHATE (2 entities in total)
• 機能のキーワード: hsp104, clpb, protein disaggregase, molecular chaperone, aaa+, atpase, cryo-em, chaperone
• 由来する生物種: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 600367.33

構造登録者

Lee, S.,Rho, S.H.,Lee, J.,Sung, N.,Liu, J.,Tsai, F.T.F. (登録日: 2018-11-30, 公開日: 2019-01-02, 最終更新日: 2024-10-16)

主引用文献

Lee, S.,Roh, S.H.,Lee, J.,Sung, N.,Liu, J.,Tsai, F.T.F.
Cryo-EM Structures of the Hsp104 Protein Disaggregase Captured in the ATP Conformation.
Cell Rep, 26:29-36.e3, 2019

PubMed 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) in the ATP-bound state determined between 7.7 Å and 9.3 Å resolution. Surprisingly, we observe that the Hsp104 hexamer adopts distinct ring conformations (closed, extended, and open) despite being in the same nucleotide state. The latter underscores the structural plasticity of Hsp104 in solution, with different conformations stabilized by nucleotide binding. Our findings suggest that, in addition to ATP hydrolysis-driven conformational changes, Hsp104 uses stochastic motions to translocate unfolded polypeptides.

PubMed: 30605683
DOI: 10.1016/j.celrep.2018.12.037

実験手法

ELECTRON MICROSCOPY (9.3 Å)