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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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
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Lenguaje:EN
Publicado: Nature Portfolio 2018
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Acceso en línea:https://doaj.org/article/f10a7d63f3934077acd63c3f83c2cc21
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spelling oai:doaj.org-article:f10a7d63f3934077acd63c3f83c2cc212021-12-02T14:41:29ZDynamic structural states of ClpB involved in its disaggregation function10.1038/s41467-018-04587-w2041-1723https://doaj.org/article/f10a7d63f3934077acd63c3f83c2cc212018-06-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-04587-whttps://doaj.org/toc/2041-1723The 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.Takayuki UchihashiYo-hei WatanabeYosuke NakazakiTakashi YamasakiHiroki WatanabeTakahiro MarunoKentaro IshiiSusumu UchiyamaChihong SongKazuyoshi MurataRyota IinoToshio AndoNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-12 (2018)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
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
Dynamic structural states of ClpB involved in its disaggregation function
description 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.
format article
author 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
author_facet 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
author_sort Takayuki Uchihashi
title Dynamic structural states of ClpB involved in its disaggregation function
title_short Dynamic structural states of ClpB involved in its disaggregation function
title_full Dynamic structural states of ClpB involved in its disaggregation function
title_fullStr Dynamic structural states of ClpB involved in its disaggregation function
title_full_unstemmed Dynamic structural states of ClpB involved in its disaggregation function
title_sort dynamic structural states of clpb involved in its disaggregation function
publisher Nature Portfolio
publishDate 2018
url https://doaj.org/article/f10a7d63f3934077acd63c3f83c2cc21
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