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Cryo-EM structure of the homohexameric T3SS ATPase-central stalk complex reveals rotary ATPase-like asymmetry
Many Gram-negative bacteria, including causative agents of dysentery, plague, and typhoid fever, rely on a type III secretion system – a multi-membrane spanning syringe-like apparatus – for their pathogenicity. The cytosolic ATPase complex of this injectisome is proposed to play an important role in...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6367419/ https://www.ncbi.nlm.nih.gov/pubmed/30733444 http://dx.doi.org/10.1038/s41467-019-08477-7 |
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author | Majewski, Dorothy D. Worrall, Liam J. Hong, Chuan Atkinson, Claire E. Vuckovic, Marija Watanabe, Nobuhiko Yu, Zhiheng Strynadka, Natalie C. J. |
author_facet | Majewski, Dorothy D. Worrall, Liam J. Hong, Chuan Atkinson, Claire E. Vuckovic, Marija Watanabe, Nobuhiko Yu, Zhiheng Strynadka, Natalie C. J. |
author_sort | Majewski, Dorothy D. |
collection | PubMed |
description | Many Gram-negative bacteria, including causative agents of dysentery, plague, and typhoid fever, rely on a type III secretion system – a multi-membrane spanning syringe-like apparatus – for their pathogenicity. The cytosolic ATPase complex of this injectisome is proposed to play an important role in energizing secretion events and substrate recognition. We present the 3.3 Å resolution cryo-EM structure of the enteropathogenic Escherichia coli ATPase EscN in complex with its central stalk EscO. The structure shows an asymmetric pore with different functional states captured in its six catalytic sites, details directly supporting a rotary catalytic mechanism analogous to that of the heterohexameric F(1)/V(1)-ATPases despite its homohexameric nature. Situated at the C-terminal opening of the EscN pore is one molecule of EscO, with primary interaction mediated through an electrostatic interface. The EscN-EscO structure provides significant atomic insights into how the ATPase contributes to type III secretion, including torque generation and binding of chaperone/substrate complexes. |
format | Online Article Text |
id | pubmed-6367419 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-63674192019-02-11 Cryo-EM structure of the homohexameric T3SS ATPase-central stalk complex reveals rotary ATPase-like asymmetry Majewski, Dorothy D. Worrall, Liam J. Hong, Chuan Atkinson, Claire E. Vuckovic, Marija Watanabe, Nobuhiko Yu, Zhiheng Strynadka, Natalie C. J. Nat Commun Article Many Gram-negative bacteria, including causative agents of dysentery, plague, and typhoid fever, rely on a type III secretion system – a multi-membrane spanning syringe-like apparatus – for their pathogenicity. The cytosolic ATPase complex of this injectisome is proposed to play an important role in energizing secretion events and substrate recognition. We present the 3.3 Å resolution cryo-EM structure of the enteropathogenic Escherichia coli ATPase EscN in complex with its central stalk EscO. The structure shows an asymmetric pore with different functional states captured in its six catalytic sites, details directly supporting a rotary catalytic mechanism analogous to that of the heterohexameric F(1)/V(1)-ATPases despite its homohexameric nature. Situated at the C-terminal opening of the EscN pore is one molecule of EscO, with primary interaction mediated through an electrostatic interface. The EscN-EscO structure provides significant atomic insights into how the ATPase contributes to type III secretion, including torque generation and binding of chaperone/substrate complexes. Nature Publishing Group UK 2019-02-07 /pmc/articles/PMC6367419/ /pubmed/30733444 http://dx.doi.org/10.1038/s41467-019-08477-7 Text en © The Author(s) 2019 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Majewski, Dorothy D. Worrall, Liam J. Hong, Chuan Atkinson, Claire E. Vuckovic, Marija Watanabe, Nobuhiko Yu, Zhiheng Strynadka, Natalie C. J. Cryo-EM structure of the homohexameric T3SS ATPase-central stalk complex reveals rotary ATPase-like asymmetry |
title | 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_short | 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 |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6367419/ https://www.ncbi.nlm.nih.gov/pubmed/30733444 http://dx.doi.org/10.1038/s41467-019-08477-7 |
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