The role of membrane destabilisation and protein dynamics in BAM catalysed OMP folding

The role of membrane destabilisation and protein dynamics in BAM catalysed OMP folding

The folding of outer membrane proteins (OMPs) is catalyzed by the βbarrel assembly machinery (BAM). Here, structural and functional analyses of BAM stabilized in distinct conformations elucidate the roles of lateral gate opening and interactions of BAM with the lipid bilayer in OMP assembly.

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Autores principales: Paul White, Samuel F. Haysom, Matthew G. Iadanza, Anna J. Higgins, Jonathan M. Machin, James M. Whitehouse, Jim E. Horne, Bob Schiffrin, Charlotte Carpenter-Platt, Antonio N. Calabrese, Kelly M. Storek, Steven T. Rutherford, David J. Brockwell, Neil A. Ranson, Sheena E. Radford
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Lenguaje:EN
Publicado: Nature Portfolio 2021
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Acceso en línea:https://doaj.org/article/bf4f9d65548640299d6a3b164c8b8b9d
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spelling oai:doaj.org-article:bf4f9d65548640299d6a3b164c8b8b9d2021-12-02T16:15:08ZThe role of membrane destabilisation and protein dynamics in BAM catalysed OMP folding10.1038/s41467-021-24432-x2041-1723https://doaj.org/article/bf4f9d65548640299d6a3b164c8b8b9d2021-07-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-24432-xhttps://doaj.org/toc/2041-1723The folding of outer membrane proteins (OMPs) is catalyzed by the βbarrel assembly machinery (BAM). Here, structural and functional analyses of BAM stabilized in distinct conformations elucidate the roles of lateral gate opening and interactions of BAM with the lipid bilayer in OMP assembly.Paul WhiteSamuel F. HaysomMatthew G. IadanzaAnna J. HigginsJonathan M. MachinJames M. WhitehouseJim E. HorneBob SchiffrinCharlotte Carpenter-PlattAntonio N. CalabreseKelly M. StorekSteven T. RutherfordDavid J. BrockwellNeil A. RansonSheena E. RadfordNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-13 (2021)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Paul White
Samuel F. Haysom
Matthew G. Iadanza
Anna J. Higgins
Jonathan M. Machin
James M. Whitehouse
Jim E. Horne
Bob Schiffrin
Charlotte Carpenter-Platt
Antonio N. Calabrese
Kelly M. Storek
Steven T. Rutherford
David J. Brockwell
Neil A. Ranson
Sheena E. Radford
The role of membrane destabilisation and protein dynamics in BAM catalysed OMP folding
description The folding of outer membrane proteins (OMPs) is catalyzed by the βbarrel assembly machinery (BAM). Here, structural and functional analyses of BAM stabilized in distinct conformations elucidate the roles of lateral gate opening and interactions of BAM with the lipid bilayer in OMP assembly.
format article
author Paul White
Samuel F. Haysom
Matthew G. Iadanza
Anna J. Higgins
Jonathan M. Machin
James M. Whitehouse
Jim E. Horne
Bob Schiffrin
Charlotte Carpenter-Platt
Antonio N. Calabrese
Kelly M. Storek
Steven T. Rutherford
David J. Brockwell
Neil A. Ranson
Sheena E. Radford
author_facet Paul White
Samuel F. Haysom
Matthew G. Iadanza
Anna J. Higgins
Jonathan M. Machin
James M. Whitehouse
Jim E. Horne
Bob Schiffrin
Charlotte Carpenter-Platt
Antonio N. Calabrese
Kelly M. Storek
Steven T. Rutherford
David J. Brockwell
Neil A. Ranson
Sheena E. Radford
author_sort Paul White
title The role of membrane destabilisation and protein dynamics in BAM catalysed OMP folding
title_short The role of membrane destabilisation and protein dynamics in BAM catalysed OMP folding
title_full The role of membrane destabilisation and protein dynamics in BAM catalysed OMP folding
title_fullStr The role of membrane destabilisation and protein dynamics in BAM catalysed OMP folding
title_full_unstemmed The role of membrane destabilisation and protein dynamics in BAM catalysed OMP folding
title_sort role of membrane destabilisation and protein dynamics in bam catalysed omp folding
publisher Nature Portfolio
publishDate 2021
url https://doaj.org/article/bf4f9d65548640299d6a3b164c8b8b9d
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