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.
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2019-02-01
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Online Access: | https://doi.org/10.1038/s41467-019-08477-7 |
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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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