Structures of chaperone-substrate complexes docked onto the export gate in a type III secretion system

Bacterial flagella are composed of proteins secreted by a type III secretion system (T3SS), which requires the action of dedicated chaperones. Here, Xing et al. report the structures of two ternary complexes among flagellar chaperones, flagellar protein substrates, and the export gate platform prote...

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Auteurs principaux:	Qiong Xing, Ke Shi, Athina Portaliou, Paolo Rossi, Anastassios Economou, Charalampos G. Kalodimos
Format:	article
Langue:	EN
Publié:	Nature Portfolio 2018
Sujets:	Science Q
Accès en ligne:	https://doaj.org/article/3301e93fb2734ce796a0783e8b545527
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id	oai:doaj.org-article:3301e93fb2734ce796a0783e8b545527
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spelling	oai:doaj.org-article:3301e93fb2734ce796a0783e8b5455272021-12-02T17:33:04ZStructures of chaperone-substrate complexes docked onto the export gate in a type III secretion system10.1038/s41467-018-04137-42041-1723https://doaj.org/article/3301e93fb2734ce796a0783e8b5455272018-05-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-04137-4https://doaj.org/toc/2041-1723Bacterial flagella are composed of proteins secreted by a type III secretion system (T3SS), which requires the action of dedicated chaperones. Here, Xing et al. report the structures of two ternary complexes among flagellar chaperones, flagellar protein substrates, and the export gate platform protein.Qiong XingKe ShiAthina PortaliouPaolo RossiAnastassios EconomouCharalampos G. KalodimosNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-9 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Qiong Xing Ke Shi Athina Portaliou Paolo Rossi Anastassios Economou Charalampos G. Kalodimos Structures of chaperone-substrate complexes docked onto the export gate in a type III secretion system
description	Bacterial flagella are composed of proteins secreted by a type III secretion system (T3SS), which requires the action of dedicated chaperones. Here, Xing et al. report the structures of two ternary complexes among flagellar chaperones, flagellar protein substrates, and the export gate platform protein.
format	article
author	Qiong Xing Ke Shi Athina Portaliou Paolo Rossi Anastassios Economou Charalampos G. Kalodimos
author_facet	Qiong Xing Ke Shi Athina Portaliou Paolo Rossi Anastassios Economou Charalampos G. Kalodimos
author_sort	Qiong Xing
title	Structures of chaperone-substrate complexes docked onto the export gate in a type III secretion system
title_short	Structures of chaperone-substrate complexes docked onto the export gate in a type III secretion system
title_full	Structures of chaperone-substrate complexes docked onto the export gate in a type III secretion system
title_fullStr	Structures of chaperone-substrate complexes docked onto the export gate in a type III secretion system
title_full_unstemmed	Structures of chaperone-substrate complexes docked onto the export gate in a type III secretion system
title_sort	structures of chaperone-substrate complexes docked onto the export gate in a type iii secretion system
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/3301e93fb2734ce796a0783e8b545527
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Structures of chaperone-substrate complexes docked onto the export gate in a type III secretion system

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