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

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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Main Authors: Qiong Xing, Ke Shi, Athina Portaliou, Paolo Rossi, Anastassios Economou, Charalampos G. Kalodimos
Format: Article
Language:English
Published: Nature Publishing Group 2018-05-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-018-04137-4
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spelling doaj-3301e93fb2734ce796a0783e8b5455272021-05-11T10:14:05ZengNature Publishing GroupNature Communications2041-17232018-05-01911910.1038/s41467-018-04137-4Structures of chaperone-substrate complexes docked onto the export gate in a type III secretion systemQiong Xing0Ke Shi1Athina Portaliou2Paolo Rossi3Anastassios Economou4Charalampos G. Kalodimos5Department of Structural Biology, St. Jude Children’s Research HospitalDepartment of Biochemistry, Molecular Biology & Biophysics, University of MinnesotaLaboratory of Molecular Bacteriology, Department of Microbiology & Immunology, Rega Institute for Medical Research, Katholicke Universiteit LeuvenDepartment of Structural Biology, St. Jude Children’s Research HospitalLaboratory of Molecular Bacteriology, Department of Microbiology & Immunology, Rega Institute for Medical Research, Katholicke Universiteit LeuvenDepartment of Structural Biology, St. Jude Children’s Research HospitalBacterial 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.https://doi.org/10.1038/s41467-018-04137-4
collection DOAJ
language English
format Article
sources DOAJ
author Qiong Xing
Ke Shi
Athina Portaliou
Paolo Rossi
Anastassios Economou
Charalampos G. Kalodimos
spellingShingle 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
Nature Communications
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 Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2018-05-01
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.
url https://doi.org/10.1038/s41467-018-04137-4
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AT athinaportaliou structuresofchaperonesubstratecomplexesdockedontotheexportgateinatypeiiisecretionsystem
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