Distortion of the bilayer and dynamics of the BAM complex in lipid nanodiscs

With cryo-EM, single-molecule FRET and MD simulations, Iadanza et al. characterise the membrane protein insertase complex BAM in lipid bilayer nanodiscs. They show that the β-barrel domain of BamA is in a ‘lateral open’ conformation, and that BAM-containing lipid nanodisc deform around BAM’s lateral...

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Autores principales:	Matthew G. Iadanza, Bob Schiffrin, Paul White, Matthew A. Watson, Jim E. Horne, Anna J. Higgins, Antonio N. Calabrese, David J. Brockwell, Roman Tuma, Antreas C. Kalli, Sheena E. Radford, Neil A. Ranson
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/cc183779d41f4d5aabd191eaa4c934aa
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spelling	oai:doaj.org-article:cc183779d41f4d5aabd191eaa4c934aa2021-12-02T12:40:39ZDistortion of the bilayer and dynamics of the BAM complex in lipid nanodiscs10.1038/s42003-020-01419-w2399-3642https://doaj.org/article/cc183779d41f4d5aabd191eaa4c934aa2020-12-01T00:00:00Zhttps://doi.org/10.1038/s42003-020-01419-whttps://doaj.org/toc/2399-3642With cryo-EM, single-molecule FRET and MD simulations, Iadanza et al. characterise the membrane protein insertase complex BAM in lipid bilayer nanodiscs. They show that the β-barrel domain of BamA is in a ‘lateral open’ conformation, and that BAM-containing lipid nanodisc deform around BAM’s lateral gate, giving structural evidence for lipid ‘disruptase’ activity of BAM.Matthew G. IadanzaBob SchiffrinPaul WhiteMatthew A. WatsonJim E. HorneAnna J. HigginsAntonio N. CalabreseDavid J. BrockwellRoman TumaAntreas C. KalliSheena E. RadfordNeil A. RansonNature PortfolioarticleBiology (General)QH301-705.5ENCommunications Biology, Vol 3, Iss 1, Pp 1-14 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 Matthew G. Iadanza Bob Schiffrin Paul White Matthew A. Watson Jim E. Horne Anna J. Higgins Antonio N. Calabrese David J. Brockwell Roman Tuma Antreas C. Kalli Sheena E. Radford Neil A. Ranson Distortion of the bilayer and dynamics of the BAM complex in lipid nanodiscs
description	With cryo-EM, single-molecule FRET and MD simulations, Iadanza et al. characterise the membrane protein insertase complex BAM in lipid bilayer nanodiscs. They show that the β-barrel domain of BamA is in a ‘lateral open’ conformation, and that BAM-containing lipid nanodisc deform around BAM’s lateral gate, giving structural evidence for lipid ‘disruptase’ activity of BAM.
format	article
author	Matthew G. Iadanza Bob Schiffrin Paul White Matthew A. Watson Jim E. Horne Anna J. Higgins Antonio N. Calabrese David J. Brockwell Roman Tuma Antreas C. Kalli Sheena E. Radford Neil A. Ranson
author_facet	Matthew G. Iadanza Bob Schiffrin Paul White Matthew A. Watson Jim E. Horne Anna J. Higgins Antonio N. Calabrese David J. Brockwell Roman Tuma Antreas C. Kalli Sheena E. Radford Neil A. Ranson
author_sort	Matthew G. Iadanza
title	Distortion of the bilayer and dynamics of the BAM complex in lipid nanodiscs
title_short	Distortion of the bilayer and dynamics of the BAM complex in lipid nanodiscs
title_full	Distortion of the bilayer and dynamics of the BAM complex in lipid nanodiscs
title_fullStr	Distortion of the bilayer and dynamics of the BAM complex in lipid nanodiscs
title_full_unstemmed	Distortion of the bilayer and dynamics of the BAM complex in lipid nanodiscs
title_sort	distortion of the bilayer and dynamics of the bam complex in lipid nanodiscs
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/cc183779d41f4d5aabd191eaa4c934aa
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Distortion of the bilayer and dynamics of the BAM complex in lipid nanodiscs

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