Formation of the β-barrel assembly machinery complex in lipid bilayers as seen by solid-state NMR

The β-barrel assembly machinery (BAM) catalyzes β-barrel protein insertion into the outer membrane of E.coli. Here authors employ high-sensitivity solid-state NMR to reveal how the lipid environment and formation of the BamA-BamCDE complex affect BamA structure and dynamics with regards to the later...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: Cecilia Pinto, Deni Mance, Tessa Sinnige, Mark Daniëls, Markus Weingarth, Marc Baldus
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2018
Materias:
Q
Acceso en línea:https://doaj.org/article/1613a33f79534e7681b9d43ef300dc17
Etiquetas: Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
id oai:doaj.org-article:1613a33f79534e7681b9d43ef300dc17
record_format dspace
spelling oai:doaj.org-article:1613a33f79534e7681b9d43ef300dc172021-12-02T17:31:58ZFormation of the β-barrel assembly machinery complex in lipid bilayers as seen by solid-state NMR10.1038/s41467-018-06466-w2041-1723https://doaj.org/article/1613a33f79534e7681b9d43ef300dc172018-10-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-06466-whttps://doaj.org/toc/2041-1723The β-barrel assembly machinery (BAM) catalyzes β-barrel protein insertion into the outer membrane of E.coli. Here authors employ high-sensitivity solid-state NMR to reveal how the lipid environment and formation of the BamA-BamCDE complex affect BamA structure and dynamics with regards to the lateral gate and the β-barrel associated domains.Cecilia PintoDeni ManceTessa SinnigeMark DaniëlsMarkus WeingarthMarc BaldusNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-10 (2018)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Cecilia Pinto
Deni Mance
Tessa Sinnige
Mark Daniëls
Markus Weingarth
Marc Baldus
Formation of the β-barrel assembly machinery complex in lipid bilayers as seen by solid-state NMR
description The β-barrel assembly machinery (BAM) catalyzes β-barrel protein insertion into the outer membrane of E.coli. Here authors employ high-sensitivity solid-state NMR to reveal how the lipid environment and formation of the BamA-BamCDE complex affect BamA structure and dynamics with regards to the lateral gate and the β-barrel associated domains.
format article
author Cecilia Pinto
Deni Mance
Tessa Sinnige
Mark Daniëls
Markus Weingarth
Marc Baldus
author_facet Cecilia Pinto
Deni Mance
Tessa Sinnige
Mark Daniëls
Markus Weingarth
Marc Baldus
author_sort Cecilia Pinto
title Formation of the β-barrel assembly machinery complex in lipid bilayers as seen by solid-state NMR
title_short Formation of the β-barrel assembly machinery complex in lipid bilayers as seen by solid-state NMR
title_full Formation of the β-barrel assembly machinery complex in lipid bilayers as seen by solid-state NMR
title_fullStr Formation of the β-barrel assembly machinery complex in lipid bilayers as seen by solid-state NMR
title_full_unstemmed Formation of the β-barrel assembly machinery complex in lipid bilayers as seen by solid-state NMR
title_sort formation of the β-barrel assembly machinery complex in lipid bilayers as seen by solid-state nmr
publisher Nature Portfolio
publishDate 2018
url https://doaj.org/article/1613a33f79534e7681b9d43ef300dc17
work_keys_str_mv AT ceciliapinto formationofthebbarrelassemblymachinerycomplexinlipidbilayersasseenbysolidstatenmr
AT denimance formationofthebbarrelassemblymachinerycomplexinlipidbilayersasseenbysolidstatenmr
AT tessasinnige formationofthebbarrelassemblymachinerycomplexinlipidbilayersasseenbysolidstatenmr
AT markdaniels formationofthebbarrelassemblymachinerycomplexinlipidbilayersasseenbysolidstatenmr
AT markusweingarth formationofthebbarrelassemblymachinerycomplexinlipidbilayersasseenbysolidstatenmr
AT marcbaldus formationofthebbarrelassemblymachinerycomplexinlipidbilayersasseenbysolidstatenmr
_version_ 1718380413365256192