Inter-domain dynamics in the chaperone SurA and multi-site binding to its outer membrane protein clients

The chaperone SurA is involved in outer membrane protein (OMP) biogenesis in Gram-negative bacteria, but its mechanism of action is not fully understood. Combining mass spectrometric, biophysical and computational approaches, the authors here show how the conformational dynamics of SurA facilitate O...

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Autores principales:	Antonio N. Calabrese, Bob Schiffrin, Matthew Watson, Theodoros K. Karamanos, Martin Walko, Julia R. Humes, Jim E. Horne, Paul White, Andrew J. Wilson, Antreas C. Kalli, Roman Tuma, Alison E. Ashcroft, David J. Brockwell, Sheena E. Radford
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/2047c9564bc341c98f0fa558c55a100a
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spelling	oai:doaj.org-article:2047c9564bc341c98f0fa558c55a100a2021-12-02T15:39:29ZInter-domain dynamics in the chaperone SurA and multi-site binding to its outer membrane protein clients10.1038/s41467-020-15702-12041-1723https://doaj.org/article/2047c9564bc341c98f0fa558c55a100a2020-05-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-15702-1https://doaj.org/toc/2041-1723The chaperone SurA is involved in outer membrane protein (OMP) biogenesis in Gram-negative bacteria, but its mechanism of action is not fully understood. Combining mass spectrometric, biophysical and computational approaches, the authors here show how the conformational dynamics of SurA facilitate OMP binding.Antonio N. CalabreseBob SchiffrinMatthew WatsonTheodoros K. KaramanosMartin WalkoJulia R. HumesJim E. HornePaul WhiteAndrew J. WilsonAntreas C. KalliRoman TumaAlison E. AshcroftDavid J. BrockwellSheena E. RadfordNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-16 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Antonio N. Calabrese Bob Schiffrin Matthew Watson Theodoros K. Karamanos Martin Walko Julia R. Humes Jim E. Horne Paul White Andrew J. Wilson Antreas C. Kalli Roman Tuma Alison E. Ashcroft David J. Brockwell Sheena E. Radford Inter-domain dynamics in the chaperone SurA and multi-site binding to its outer membrane protein clients
description	The chaperone SurA is involved in outer membrane protein (OMP) biogenesis in Gram-negative bacteria, but its mechanism of action is not fully understood. Combining mass spectrometric, biophysical and computational approaches, the authors here show how the conformational dynamics of SurA facilitate OMP binding.
format	article
author	Antonio N. Calabrese Bob Schiffrin Matthew Watson Theodoros K. Karamanos Martin Walko Julia R. Humes Jim E. Horne Paul White Andrew J. Wilson Antreas C. Kalli Roman Tuma Alison E. Ashcroft David J. Brockwell Sheena E. Radford
author_facet	Antonio N. Calabrese Bob Schiffrin Matthew Watson Theodoros K. Karamanos Martin Walko Julia R. Humes Jim E. Horne Paul White Andrew J. Wilson Antreas C. Kalli Roman Tuma Alison E. Ashcroft David J. Brockwell Sheena E. Radford
author_sort	Antonio N. Calabrese
title	Inter-domain dynamics in the chaperone SurA and multi-site binding to its outer membrane protein clients
title_short	Inter-domain dynamics in the chaperone SurA and multi-site binding to its outer membrane protein clients
title_full	Inter-domain dynamics in the chaperone SurA and multi-site binding to its outer membrane protein clients
title_fullStr	Inter-domain dynamics in the chaperone SurA and multi-site binding to its outer membrane protein clients
title_full_unstemmed	Inter-domain dynamics in the chaperone SurA and multi-site binding to its outer membrane protein clients
title_sort	inter-domain dynamics in the chaperone sura and multi-site binding to its outer membrane protein clients
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/2047c9564bc341c98f0fa558c55a100a
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Inter-domain dynamics in the chaperone SurA and multi-site binding to its outer membrane protein clients

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