Spectroscopic glimpses of the transition state of ATP hydrolysis trapped in a bacterial DnaB helicase

Here, the authors use solid-state NMR and EPR measurements to characterise the ATP hydrolysis transition state of the oligomeric bacterial DnaB helicase from Helicobacter pylori, which was trapped by using aluminium fluoride as a chemical mimic. They identify protein protons that coordinate to the p...

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Autores principales: Alexander A. Malär, Nino Wili, Laura A. Völker, Maria I. Kozlova, Riccardo Cadalbert, Alexander Däpp, Marco E. Weber, Johannes Zehnder, Gunnar Jeschke, Hellmut Eckert, Anja Böckmann, Daniel Klose, Armen Y. Mulkidjanian, Beat H. Meier, Thomas Wiegand
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Lenguaje:EN
Publicado: Nature Portfolio 2021
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Acceso en línea:https://doaj.org/article/eb891282fac642d58cd86a545184715e
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spelling oai:doaj.org-article:eb891282fac642d58cd86a545184715e2021-12-02T19:12:25ZSpectroscopic glimpses of the transition state of ATP hydrolysis trapped in a bacterial DnaB helicase10.1038/s41467-021-25599-z2041-1723https://doaj.org/article/eb891282fac642d58cd86a545184715e2021-09-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-25599-zhttps://doaj.org/toc/2041-1723Here, the authors use solid-state NMR and EPR measurements to characterise the ATP hydrolysis transition state of the oligomeric bacterial DnaB helicase from Helicobacter pylori, which was trapped by using aluminium fluoride as a chemical mimic. They identify protein protons that coordinate to the phosphate groups of ADP and DNA and observe that the aluminium fluoride unit is highly mobile and fast-rotating.Alexander A. MalärNino WiliLaura A. VölkerMaria I. KozlovaRiccardo CadalbertAlexander DäppMarco E. WeberJohannes ZehnderGunnar JeschkeHellmut EckertAnja BöckmannDaniel KloseArmen Y. MulkidjanianBeat H. MeierThomas WiegandNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-13 (2021)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Alexander A. Malär
Nino Wili
Laura A. Völker
Maria I. Kozlova
Riccardo Cadalbert
Alexander Däpp
Marco E. Weber
Johannes Zehnder
Gunnar Jeschke
Hellmut Eckert
Anja Böckmann
Daniel Klose
Armen Y. Mulkidjanian
Beat H. Meier
Thomas Wiegand
Spectroscopic glimpses of the transition state of ATP hydrolysis trapped in a bacterial DnaB helicase
description Here, the authors use solid-state NMR and EPR measurements to characterise the ATP hydrolysis transition state of the oligomeric bacterial DnaB helicase from Helicobacter pylori, which was trapped by using aluminium fluoride as a chemical mimic. They identify protein protons that coordinate to the phosphate groups of ADP and DNA and observe that the aluminium fluoride unit is highly mobile and fast-rotating.
format article
author Alexander A. Malär
Nino Wili
Laura A. Völker
Maria I. Kozlova
Riccardo Cadalbert
Alexander Däpp
Marco E. Weber
Johannes Zehnder
Gunnar Jeschke
Hellmut Eckert
Anja Böckmann
Daniel Klose
Armen Y. Mulkidjanian
Beat H. Meier
Thomas Wiegand
author_facet Alexander A. Malär
Nino Wili
Laura A. Völker
Maria I. Kozlova
Riccardo Cadalbert
Alexander Däpp
Marco E. Weber
Johannes Zehnder
Gunnar Jeschke
Hellmut Eckert
Anja Böckmann
Daniel Klose
Armen Y. Mulkidjanian
Beat H. Meier
Thomas Wiegand
author_sort Alexander A. Malär
title Spectroscopic glimpses of the transition state of ATP hydrolysis trapped in a bacterial DnaB helicase
title_short Spectroscopic glimpses of the transition state of ATP hydrolysis trapped in a bacterial DnaB helicase
title_full Spectroscopic glimpses of the transition state of ATP hydrolysis trapped in a bacterial DnaB helicase
title_fullStr Spectroscopic glimpses of the transition state of ATP hydrolysis trapped in a bacterial DnaB helicase
title_full_unstemmed Spectroscopic glimpses of the transition state of ATP hydrolysis trapped in a bacterial DnaB helicase
title_sort spectroscopic glimpses of the transition state of atp hydrolysis trapped in a bacterial dnab helicase
publisher Nature Portfolio
publishDate 2021
url https://doaj.org/article/eb891282fac642d58cd86a545184715e
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