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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Autores principales: Qiong Xing, Ke Shi, Athina Portaliou, Paolo Rossi, Anastassios Economou, Charalampos G. Kalodimos
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2018
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Acceso en línea:https://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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