Cryo-EM structure of the homohexameric T3SS ATPase-central stalk complex reveals rotary ATPase-like asymmetry

Many Gram-negative bacteria rely on a type III secretion system (T3SS) for their pathogenicity. Here authors present the cryo-EM structure of the E.coli T3SS ATPase-central stalk complex, which forms a homohexameric, asymmetric pore with different functional states.

Bibliographic Details
Main Authors: Dorothy D. Majewski, Liam J. Worrall, Chuan Hong, Claire E. Atkinson, Marija Vuckovic, Nobuhiko Watanabe, Zhiheng Yu, Natalie C. J. Strynadka
Format: Article
Language:English
Published: Nature Publishing Group 2019-02-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-019-08477-7
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spelling doaj-655ed92072524851b04d71448b77be1e2021-05-11T12:18:57ZengNature Publishing GroupNature Communications2041-17232019-02-0110111210.1038/s41467-019-08477-7Cryo-EM structure of the homohexameric T3SS ATPase-central stalk complex reveals rotary ATPase-like asymmetryDorothy D. Majewski0Liam J. Worrall1Chuan Hong2Claire E. Atkinson3Marija Vuckovic4Nobuhiko Watanabe5Zhiheng Yu6Natalie C. J. Strynadka7Department of Biochemistry and Molecular Biology and the Center for Blood Research, University of British ColumbiaDepartment of Biochemistry and Molecular Biology and the Center for Blood Research, University of British ColumbiaCryoEM Shared Resources, Howard Hughes Medical InstituteDepartment of Biochemistry and Molecular Biology and the Center for Blood Research, University of British ColumbiaDepartment of Biochemistry and Molecular Biology and the Center for Blood Research, University of British ColumbiaDepartment of Biochemistry and Molecular Biology and the Center for Blood Research, University of British ColumbiaCryoEM Shared Resources, Howard Hughes Medical InstituteDepartment of Biochemistry and Molecular Biology and the Center for Blood Research, University of British ColumbiaMany Gram-negative bacteria rely on a type III secretion system (T3SS) for their pathogenicity. Here authors present the cryo-EM structure of the E.coli T3SS ATPase-central stalk complex, which forms a homohexameric, asymmetric pore with different functional states.https://doi.org/10.1038/s41467-019-08477-7
collection DOAJ
language English
format Article
sources DOAJ
author Dorothy D. Majewski
Liam J. Worrall
Chuan Hong
Claire E. Atkinson
Marija Vuckovic
Nobuhiko Watanabe
Zhiheng Yu
Natalie C. J. Strynadka
spellingShingle Dorothy D. Majewski
Liam J. Worrall
Chuan Hong
Claire E. Atkinson
Marija Vuckovic
Nobuhiko Watanabe
Zhiheng Yu
Natalie C. J. Strynadka
Cryo-EM structure of the homohexameric T3SS ATPase-central stalk complex reveals rotary ATPase-like asymmetry
Nature Communications
author_facet Dorothy D. Majewski
Liam J. Worrall
Chuan Hong
Claire E. Atkinson
Marija Vuckovic
Nobuhiko Watanabe
Zhiheng Yu
Natalie C. J. Strynadka
author_sort Dorothy D. Majewski
title Cryo-EM structure of the homohexameric T3SS ATPase-central stalk complex reveals rotary ATPase-like asymmetry
title_short Cryo-EM structure of the homohexameric T3SS ATPase-central stalk complex reveals rotary ATPase-like asymmetry
title_full Cryo-EM structure of the homohexameric T3SS ATPase-central stalk complex reveals rotary ATPase-like asymmetry
title_fullStr Cryo-EM structure of the homohexameric T3SS ATPase-central stalk complex reveals rotary ATPase-like asymmetry
title_full_unstemmed Cryo-EM structure of the homohexameric T3SS ATPase-central stalk complex reveals rotary ATPase-like asymmetry
title_sort cryo-em structure of the homohexameric t3ss atpase-central stalk complex reveals rotary atpase-like asymmetry
publisher Nature Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2019-02-01
description Many Gram-negative bacteria rely on a type III secretion system (T3SS) for their pathogenicity. Here authors present the cryo-EM structure of the E.coli T3SS ATPase-central stalk complex, which forms a homohexameric, asymmetric pore with different functional states.
url https://doi.org/10.1038/s41467-019-08477-7
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