5ZUI

Crystal Structure of HSP104 from Chaetomium thermophilum

5ZUI の概要

• エントリーDOI: 10.2210/pdb5zui/pdb
• 分子名称: Heat Shock Protein 104, ADENOSINE-5'-DIPHOSPHATE, SULFATE ION, ... (4 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
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 86486.85

構造登録者

Hanazono, Y.,Inoue, Y.,Noguchi, K.,Yohda, M.,Shinohara, K.,Takeda, K.,Miki, K. (登録日: 2018-05-07, 公開日: 2019-06-19, 最終更新日: 2023-11-22)

主引用文献

Inoue, Y.,Hanazono, Y.,Noi, K.,Kawamoto, A.,Kimatsuka, M.,Harada, R.,Takeda, K.,Kita, R.,Iwamasa, N.,Shibata, K.,Noguchi, K.,Shigeta, Y.,Namba, K.,Ogura, T.,Miki, K.,Shinohara, K.,Yohda, M.
Split conformation of Chaetomium thermophilum Hsp104 disaggregase.
Structure, 2021

PubMed Abstract: Hsp104 and its bacterial homolog ClpB form hexameric ring structures and mediate protein disaggregation. The disaggregated polypeptide is thought to thread through the central channel of the ring. However, the dynamic behavior of Hsp104 during disaggregation remains unclear. Here, we reported the stochastic conformational dynamics and a split conformation of Hsp104 disaggregase from Chaetomium thermophilum (CtHsp104) in the presence of ADP by X-ray crystallography, cryo-electron microscopy (EM), and high-speed atomic force microscopy (AFM). ADP-bound CtHsp104 assembles into a 6 left-handed spiral filament in the crystal structure at a resolution of 2.7 Å. The unit of the filament is a hexamer of the split spiral structure. In the cryo-EM images, staggered and split hexameric rings were observed. Further, high-speed AFM observations showed that a substrate addition enhanced the conformational change and increased the split structure's frequency. Our data suggest that split conformation is an off-pathway state of CtHsp104 during disaggregation.

PubMed: 33651974
DOI: 10.1016/j.str.2021.02.002

実験手法

X-RAY DIFFRACTION (2.701 Å)