Structural basis for substrate gripping and translocation by the ClpB AAA+ disaggregase

Bacterial ClpB is a disaggregase that solubilizes protein aggregates. Here the authors present the 2.9 Å cryo-EM structure of a hyperactive variant of ClpB bound to the substrate casein in active translocation states and discuss its polypeptide translocation mechanism.

Bibliographic Details
Main Authors:	Alexandrea N. Rizo, JiaBei Lin, Stephanie N. Gates, Eric Tse, Stephen M. Bart, Laura M. Castellano, Frank DiMaio, James Shorter, Daniel R. Southworth
Format:	Article
Language:	English
Published:	Nature Publishing Group 2019-06-01
Series:	Nature Communications
Online Access:	https://doi.org/10.1038/s41467-019-10150-y

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spelling	doaj-4b26b48e90114f5a86fdb8eed991c1302021-05-11T12:27:33ZengNature Publishing GroupNature Communications2041-17232019-06-0110111210.1038/s41467-019-10150-yStructural basis for substrate gripping and translocation by the ClpB AAA+ disaggregaseAlexandrea N. Rizo0JiaBei Lin1Stephanie N. Gates2Eric Tse3Stephen M. Bart4Laura M. Castellano5Frank DiMaio6James Shorter7Daniel R. Southworth8Graduate Program in Chemical Biology, University of MichiganDepartment of Biochemistry and Biophysics, Perelman School of Medicine at the University of PennsylvaniaGraduate Program in Chemical Biology, University of MichiganDepartment of Biochemistry and Biophysics, Institute for Neurodegenerative Diseases, University of CaliforniaDepartment of Biochemistry and Biophysics, Perelman School of Medicine at the University of PennsylvaniaDepartment of Biochemistry and Biophysics, Perelman School of Medicine at the University of PennsylvaniaDepartment of Biochemistry, University of WashingtonDepartment of Biochemistry and Biophysics, Perelman School of Medicine at the University of PennsylvaniaDepartment of Biochemistry and Biophysics, Institute for Neurodegenerative Diseases, University of CaliforniaBacterial ClpB is a disaggregase that solubilizes protein aggregates. Here the authors present the 2.9 Å cryo-EM structure of a hyperactive variant of ClpB bound to the substrate casein in active translocation states and discuss its polypeptide translocation mechanism.https://doi.org/10.1038/s41467-019-10150-y
collection	DOAJ
language	English
format	Article
sources	DOAJ
author	Alexandrea N. Rizo JiaBei Lin Stephanie N. Gates Eric Tse Stephen M. Bart Laura M. Castellano Frank DiMaio James Shorter Daniel R. Southworth
spellingShingle	Alexandrea N. Rizo JiaBei Lin Stephanie N. Gates Eric Tse Stephen M. Bart Laura M. Castellano Frank DiMaio James Shorter Daniel R. Southworth Structural basis for substrate gripping and translocation by the ClpB AAA+ disaggregase Nature Communications
author_facet	Alexandrea N. Rizo JiaBei Lin Stephanie N. Gates Eric Tse Stephen M. Bart Laura M. Castellano Frank DiMaio James Shorter Daniel R. Southworth
author_sort	Alexandrea N. Rizo
title	Structural basis for substrate gripping and translocation by the ClpB AAA+ disaggregase
title_short	Structural basis for substrate gripping and translocation by the ClpB AAA+ disaggregase
title_full	Structural basis for substrate gripping and translocation by the ClpB AAA+ disaggregase
title_fullStr	Structural basis for substrate gripping and translocation by the ClpB AAA+ disaggregase
title_full_unstemmed	Structural basis for substrate gripping and translocation by the ClpB AAA+ disaggregase
title_sort	structural basis for substrate gripping and translocation by the clpb aaa+ disaggregase
publisher	Nature Publishing Group
series	Nature Communications
issn	2041-1723
publishDate	2019-06-01
description	Bacterial ClpB is a disaggregase that solubilizes protein aggregates. Here the authors present the 2.9 Å cryo-EM structure of a hyperactive variant of ClpB bound to the substrate casein in active translocation states and discuss its polypeptide translocation mechanism.
url	https://doi.org/10.1038/s41467-019-10150-y
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Structural basis for substrate gripping and translocation by the ClpB AAA+ disaggregase

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