Structural basis for the homotypic fusion of chlamydial inclusions by the SNARE-like protein IncA

Chlamydia trachomatis forms membrane-bound inclusions inside the host cell that are decorated with IncA, a SNARE-like protein that promotes the fusion of inclusions. Here, Cingolani et al. show that the protein folds into a non-canonical four-helix bundle and identify an intramolecular clamp require...

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Autores principales:	Gino Cingolani, Michael McCauley, Anna Lobley, Alexander J. Bryer, Jordan Wesolowski, Deanna L. Greco, Ravi K. Lokareddy, Erik Ronzone, Juan R. Perilla, Fabienne Paumet
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/d9b4e46bb6f643ab90bbf0b252996fa0
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spelling	oai:doaj.org-article:d9b4e46bb6f643ab90bbf0b252996fa02021-12-02T16:58:28ZStructural basis for the homotypic fusion of chlamydial inclusions by the SNARE-like protein IncA10.1038/s41467-019-10806-92041-1723https://doaj.org/article/d9b4e46bb6f643ab90bbf0b252996fa02019-06-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-10806-9https://doaj.org/toc/2041-1723Chlamydia trachomatis forms membrane-bound inclusions inside the host cell that are decorated with IncA, a SNARE-like protein that promotes the fusion of inclusions. Here, Cingolani et al. show that the protein folds into a non-canonical four-helix bundle and identify an intramolecular clamp required for membrane fusion.Gino CingolaniMichael McCauleyAnna LobleyAlexander J. BryerJordan WesolowskiDeanna L. GrecoRavi K. LokareddyErik RonzoneJuan R. PerillaFabienne PaumetNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-12 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Gino Cingolani Michael McCauley Anna Lobley Alexander J. Bryer Jordan Wesolowski Deanna L. Greco Ravi K. Lokareddy Erik Ronzone Juan R. Perilla Fabienne Paumet Structural basis for the homotypic fusion of chlamydial inclusions by the SNARE-like protein IncA
description	Chlamydia trachomatis forms membrane-bound inclusions inside the host cell that are decorated with IncA, a SNARE-like protein that promotes the fusion of inclusions. Here, Cingolani et al. show that the protein folds into a non-canonical four-helix bundle and identify an intramolecular clamp required for membrane fusion.
format	article
author	Gino Cingolani Michael McCauley Anna Lobley Alexander J. Bryer Jordan Wesolowski Deanna L. Greco Ravi K. Lokareddy Erik Ronzone Juan R. Perilla Fabienne Paumet
author_facet	Gino Cingolani Michael McCauley Anna Lobley Alexander J. Bryer Jordan Wesolowski Deanna L. Greco Ravi K. Lokareddy Erik Ronzone Juan R. Perilla Fabienne Paumet
author_sort	Gino Cingolani
title	Structural basis for the homotypic fusion of chlamydial inclusions by the SNARE-like protein IncA
title_short	Structural basis for the homotypic fusion of chlamydial inclusions by the SNARE-like protein IncA
title_full	Structural basis for the homotypic fusion of chlamydial inclusions by the SNARE-like protein IncA
title_fullStr	Structural basis for the homotypic fusion of chlamydial inclusions by the SNARE-like protein IncA
title_full_unstemmed	Structural basis for the homotypic fusion of chlamydial inclusions by the SNARE-like protein IncA
title_sort	structural basis for the homotypic fusion of chlamydial inclusions by the snare-like protein inca
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/d9b4e46bb6f643ab90bbf0b252996fa0
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Structural basis for the homotypic fusion of chlamydial inclusions by the SNARE-like protein IncA

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