5D4W

Crystal structure of Hsp104

5D4W の概要

• エントリーDOI: 10.2210/pdb5d4w/pdb
• 分子名称: Putative heat shock protein, ADENOSINE-5'-DIPHOSPHATE (2 entities in total)
• 機能のキーワード: protein disaggregase, atpase, two-ring aaa protein, helical filament, chaperone
• 由来する生物種: Chaetomium thermophilum; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 314104.67

構造登録者

Heuck, A.,Schitter-Sollner, S.,Clausen, T. (登録日: 2015-08-09, 公開日: 2016-12-07, 最終更新日: 2024-11-20)

主引用文献

Heuck, A.,Schitter-Sollner, S.,Suskiewicz, M.J.,Kurzbauer, R.,Kley, J.,Schleiffer, A.,Rombaut, P.,Herzog, F.,Clausen, T.
Structural basis for the disaggregase activity and regulation of Hsp104.
Elife, 5:-, 2016

PubMed Abstract: The Hsp104 disaggregase is a two-ring ATPase machine that rescues various forms of non-native proteins including the highly resistant amyloid fibers. The structural-mechanistic underpinnings of how the recovery of toxic protein aggregates is promoted and how this potent unfolding activity is prevented from doing collateral damage to cellular proteins are not well understood. Here, we present structural and biochemical data revealing the organization of Hsp104 from at 3.7 Å resolution. We show that the coiled-coil domains encircling the disaggregase constitute a 'restraint mask' that sterically controls the mobility and thus the unfolding activity of the ATPase modules. In addition, we identify a mechanical linkage that coordinates the activity of the two ATPase rings and accounts for the high unfolding potential of Hsp104. Based on these findings, we propose a general model for how Hsp104 and related chaperones operate and are kept under control until recruited to appropriate substrates.

PubMed: 27901467
DOI: 10.7554/eLife.21516

実験手法

X-RAY DIFFRACTION (3.7 Å)