Molecular basis for the folding of β-helical autotransporter passenger domains

Autotransporter passenger domains are presented on or released from the bacterial surface upon translocation through an outer membrane β-barrel anchor. Here the authors study the two E. coli autotransporters Pet and EspP and propose that the β-barrel anchor acts as a vector to nucleate the folding o...

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Autores principales:	Xiaojun Yuan, Matthew D. Johnson, Jing Zhang, Alvin W. Lo, Mark A. Schembri, Lakshmi C. Wijeyewickrema, Robert N. Pike, Gerard H. M. Huysmans, Ian R. Henderson, Denisse L. Leyton
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/f98a1b1242774a1e9a6565cc46622c09
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spelling	oai:doaj.org-article:f98a1b1242774a1e9a6565cc46622c092021-12-02T16:49:34ZMolecular basis for the folding of β-helical autotransporter passenger domains10.1038/s41467-018-03593-22041-1723https://doaj.org/article/f98a1b1242774a1e9a6565cc46622c092018-04-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-03593-2https://doaj.org/toc/2041-1723Autotransporter passenger domains are presented on or released from the bacterial surface upon translocation through an outer membrane β-barrel anchor. Here the authors study the two E. coli autotransporters Pet and EspP and propose that the β-barrel anchor acts as a vector to nucleate the folding of the passenger domain.Xiaojun YuanMatthew D. JohnsonJing ZhangAlvin W. LoMark A. SchembriLakshmi C. WijeyewickremaRobert N. PikeGerard H. M. HuysmansIan R. HendersonDenisse L. LeytonNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-12 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Xiaojun Yuan Matthew D. Johnson Jing Zhang Alvin W. Lo Mark A. Schembri Lakshmi C. Wijeyewickrema Robert N. Pike Gerard H. M. Huysmans Ian R. Henderson Denisse L. Leyton Molecular basis for the folding of β-helical autotransporter passenger domains
description	Autotransporter passenger domains are presented on or released from the bacterial surface upon translocation through an outer membrane β-barrel anchor. Here the authors study the two E. coli autotransporters Pet and EspP and propose that the β-barrel anchor acts as a vector to nucleate the folding of the passenger domain.
format	article
author	Xiaojun Yuan Matthew D. Johnson Jing Zhang Alvin W. Lo Mark A. Schembri Lakshmi C. Wijeyewickrema Robert N. Pike Gerard H. M. Huysmans Ian R. Henderson Denisse L. Leyton
author_facet	Xiaojun Yuan Matthew D. Johnson Jing Zhang Alvin W. Lo Mark A. Schembri Lakshmi C. Wijeyewickrema Robert N. Pike Gerard H. M. Huysmans Ian R. Henderson Denisse L. Leyton
author_sort	Xiaojun Yuan
title	Molecular basis for the folding of β-helical autotransporter passenger domains
title_short	Molecular basis for the folding of β-helical autotransporter passenger domains
title_full	Molecular basis for the folding of β-helical autotransporter passenger domains
title_fullStr	Molecular basis for the folding of β-helical autotransporter passenger domains
title_full_unstemmed	Molecular basis for the folding of β-helical autotransporter passenger domains
title_sort	molecular basis for the folding of β-helical autotransporter passenger domains
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/f98a1b1242774a1e9a6565cc46622c09
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Molecular basis for the folding of β-helical autotransporter passenger domains

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