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...
Guardado en:
Autores principales: | , , , , , |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2018
|
Materias: | |
Acceso en línea: | https://doaj.org/article/3301e93fb2734ce796a0783e8b545527 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
id |
oai:doaj.org-article:3301e93fb2734ce796a0783e8b545527 |
---|---|
record_format |
dspace |
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 |
work_keys_str_mv |
AT qiongxing structuresofchaperonesubstratecomplexesdockedontotheexportgateinatypeiiisecretionsystem AT keshi structuresofchaperonesubstratecomplexesdockedontotheexportgateinatypeiiisecretionsystem AT athinaportaliou structuresofchaperonesubstratecomplexesdockedontotheexportgateinatypeiiisecretionsystem AT paolorossi structuresofchaperonesubstratecomplexesdockedontotheexportgateinatypeiiisecretionsystem AT anastassioseconomou structuresofchaperonesubstratecomplexesdockedontotheexportgateinatypeiiisecretionsystem AT charalamposgkalodimos structuresofchaperonesubstratecomplexesdockedontotheexportgateinatypeiiisecretionsystem |
_version_ |
1718380054626435072 |