Article
Dynamic structural states of ClpB involved in its disaggregation function.
Nature communications - 1 Jun 2018
Uchihashi Takayuki, Watanabe Yo-Hei, Nakazaki Yosuke, Yamasaki Takashi, Watanabe Hiroki, Maruno Takahiro, Ishii Kentaro, Uchiyama Susumu, Song Chihong, Murata Kazuyoshi, Iino Ryota, Ando Toshio
Abstract excerpt
The ATP-dependent bacterial protein disaggregation machine, ClpB belonging to the AAA+ superfamily, refolds toxic protein aggregates into the native state in cooperation with the cognate Hsp70 partner. The ring-shaped hexamers of ClpB unfold and thread its protein substrate through the central pore. However, their function-related structural dynamics has remained elusive. Here we directly visualize ClpB using...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.