@article{oai:repo.qst.go.jp:00082736,
 author = {Inoue, Yosuke and Yuya, Hanazono and Noi, Kentaro and Kawamoto, Akihiro and Kimatsuka, Masato and Harada, Ryuhei and Takeda, Kazuki and Kita, Ryoichi and Iwamasa, Natsuki and Shibata, Kyoka and Noguchi, Keiichi and Shigeta, Yasuteru and Namba, Keiichi and Ogura, Teru and Miki, Kunio and Shinohara, Kyosuke and Yohda, Masafumi and Yuya, Hanazono},
 issue = {7},
 journal = {Structure},
 month = {Apr},
 note = {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 65 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.},
 pages = {721--730},
 title = {Split conformation of Chaetomium thermophilum Hsp104 disaggregase},
 volume = {29},
 year = {2021}
}