A viral-fusion-peptide-like molecular switch drives membrane insertion of botulinum neurotoxin A1

The translocation domain (HN) of Botulinum neurotoxins (BoNTs) mediates the delivery of the BoNT light chain (LC) into neuronal cytosol. Here the authors provide insights into HN membrane insertion by determining the crystal structure of BoNT/A1 HN at acidic pH, which reveals a molecular switch in H...

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Autores principales:	Kwok-ho Lam, Zhuojun Guo, Nadja Krez, Tsutomu Matsui, Kay Perry, Jasmin Weisemann, Andreas Rummel, Mark E. Bowen, Rongsheng Jin
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/254881e40fb84f0690898f9dda9538c2
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spelling	oai:doaj.org-article:254881e40fb84f0690898f9dda9538c22021-12-02T14:38:52ZA viral-fusion-peptide-like molecular switch drives membrane insertion of botulinum neurotoxin A110.1038/s41467-018-07789-42041-1723https://doaj.org/article/254881e40fb84f0690898f9dda9538c22018-12-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-07789-4https://doaj.org/toc/2041-1723The translocation domain (HN) of Botulinum neurotoxins (BoNTs) mediates the delivery of the BoNT light chain (LC) into neuronal cytosol. Here the authors provide insights into HN membrane insertion by determining the crystal structure of BoNT/A1 HN at acidic pH, which reveals a molecular switch in HN, where buried α-helices are transformed into surface-exposed hydrophobic β-hairpins.Kwok-ho LamZhuojun GuoNadja KrezTsutomu MatsuiKay PerryJasmin WeisemannAndreas RummelMark E. BowenRongsheng JinNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-12 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Kwok-ho Lam Zhuojun Guo Nadja Krez Tsutomu Matsui Kay Perry Jasmin Weisemann Andreas Rummel Mark E. Bowen Rongsheng Jin A viral-fusion-peptide-like molecular switch drives membrane insertion of botulinum neurotoxin A1
description	The translocation domain (HN) of Botulinum neurotoxins (BoNTs) mediates the delivery of the BoNT light chain (LC) into neuronal cytosol. Here the authors provide insights into HN membrane insertion by determining the crystal structure of BoNT/A1 HN at acidic pH, which reveals a molecular switch in HN, where buried α-helices are transformed into surface-exposed hydrophobic β-hairpins.
format	article
author	Kwok-ho Lam Zhuojun Guo Nadja Krez Tsutomu Matsui Kay Perry Jasmin Weisemann Andreas Rummel Mark E. Bowen Rongsheng Jin
author_facet	Kwok-ho Lam Zhuojun Guo Nadja Krez Tsutomu Matsui Kay Perry Jasmin Weisemann Andreas Rummel Mark E. Bowen Rongsheng Jin
author_sort	Kwok-ho Lam
title	A viral-fusion-peptide-like molecular switch drives membrane insertion of botulinum neurotoxin A1
title_short	A viral-fusion-peptide-like molecular switch drives membrane insertion of botulinum neurotoxin A1
title_full	A viral-fusion-peptide-like molecular switch drives membrane insertion of botulinum neurotoxin A1
title_fullStr	A viral-fusion-peptide-like molecular switch drives membrane insertion of botulinum neurotoxin A1
title_full_unstemmed	A viral-fusion-peptide-like molecular switch drives membrane insertion of botulinum neurotoxin A1
title_sort	viral-fusion-peptide-like molecular switch drives membrane insertion of botulinum neurotoxin a1
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/254881e40fb84f0690898f9dda9538c2
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A viral-fusion-peptide-like molecular switch drives membrane insertion of botulinum neurotoxin A1

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