The conformational changes coupling ATP hydrolysis and translocation in a bacterial DnaB helicase

DnaB helicases are motor proteins that couple ATP-hydrolysis to the movement of the protein along single-stranded DNA leading to a separation of double-stranded DNA at the replication fork. Here authors use solid-state NMR spectroscopy and reveal DnaB’s conformational responses to ATP hydrolysis and...

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Autores principales:	Thomas Wiegand, Riccardo Cadalbert, Denis Lacabanne, Joanna Timmins, Laurent Terradot, Anja Böckmann, Beat H. Meier
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/c17546a852b844549ff8e421f8004bda
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spelling	oai:doaj.org-article:c17546a852b844549ff8e421f8004bda2021-12-02T16:50:59ZThe conformational changes coupling ATP hydrolysis and translocation in a bacterial DnaB helicase10.1038/s41467-018-07968-32041-1723https://doaj.org/article/c17546a852b844549ff8e421f8004bda2019-01-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-07968-3https://doaj.org/toc/2041-1723DnaB helicases are motor proteins that couple ATP-hydrolysis to the movement of the protein along single-stranded DNA leading to a separation of double-stranded DNA at the replication fork. Here authors use solid-state NMR spectroscopy and reveal DnaB’s conformational responses to ATP hydrolysis and the resulting DNA loading and translocation.Thomas WiegandRiccardo CadalbertDenis LacabanneJoanna TimminsLaurent TerradotAnja BöckmannBeat H. MeierNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-11 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Thomas Wiegand Riccardo Cadalbert Denis Lacabanne Joanna Timmins Laurent Terradot Anja Böckmann Beat H. Meier The conformational changes coupling ATP hydrolysis and translocation in a bacterial DnaB helicase
description	DnaB helicases are motor proteins that couple ATP-hydrolysis to the movement of the protein along single-stranded DNA leading to a separation of double-stranded DNA at the replication fork. Here authors use solid-state NMR spectroscopy and reveal DnaB’s conformational responses to ATP hydrolysis and the resulting DNA loading and translocation.
format	article
author	Thomas Wiegand Riccardo Cadalbert Denis Lacabanne Joanna Timmins Laurent Terradot Anja Böckmann Beat H. Meier
author_facet	Thomas Wiegand Riccardo Cadalbert Denis Lacabanne Joanna Timmins Laurent Terradot Anja Böckmann Beat H. Meier
author_sort	Thomas Wiegand
title	The conformational changes coupling ATP hydrolysis and translocation in a bacterial DnaB helicase
title_short	The conformational changes coupling ATP hydrolysis and translocation in a bacterial DnaB helicase
title_full	The conformational changes coupling ATP hydrolysis and translocation in a bacterial DnaB helicase
title_fullStr	The conformational changes coupling ATP hydrolysis and translocation in a bacterial DnaB helicase
title_full_unstemmed	The conformational changes coupling ATP hydrolysis and translocation in a bacterial DnaB helicase
title_sort	conformational changes coupling atp hydrolysis and translocation in a bacterial dnab helicase
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/c17546a852b844549ff8e421f8004bda
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The conformational changes coupling ATP hydrolysis and translocation in a bacterial DnaB helicase

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