Dynamic structural states of ClpB involved in its disaggregation function

Dynamic structural states of ClpB involved in its disaggregation function

The bacterial protein disaggregation machine ClpB uses ATP to generate mechanical force to unfold and thread its protein substrates. Here authors visualize the ClpB ring using high-speed atomic force microscopy and capture conformational changes of the hexameric ring during the ATPase reaction.

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Detalles Bibliográficos
Autores principales: Takayuki Uchihashi, Yo-hei Watanabe, Yosuke Nakazaki, Takashi Yamasaki, Hiroki Watanabe, Takahiro Maruno, Kentaro Ishii, Susumu Uchiyama, Chihong Song, Kazuyoshi Murata, Ryota Iino, Toshio Ando
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2018
Materias:
Science
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Acceso en línea:https://doaj.org/article/f10a7d63f3934077acd63c3f83c2cc21
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Sumario:The bacterial protein disaggregation machine ClpB uses ATP to generate mechanical force to unfold and thread its protein substrates. Here authors visualize the ClpB ring using high-speed atomic force microscopy and capture conformational changes of the hexameric ring during the ATPase reaction.

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