Al-Otaibi, N.S., Taylor, A.J., Farrell, D.P. et al. (4 more authors) (2020) The cryo-EM structure of the bacterial flagellum cap complex suggests a molecular mechanism for filament elongation. Nature Communications, 11 (1). 3210. ISSN 2041-1723
Abstract
The bacterial flagellum is a remarkable molecular motor, whose primary function in bacteria is to facilitate motility through the rotation of a filament protruding from the bacterial cell. A cap complex, consisting of an oligomer of the protein FliD, is localized at the tip of the flagellum, and is essential for filament assembly, as well as adherence to surfaces in some bacteria. However, the structure of the intact cap complex, and the molecular basis for its interaction with the filament, remains elusive. Here we report the cryo-EM structure of the Campylobacter jejuni cap complex, which reveals that FliD is pentameric, with the N-terminal region of the protomer forming an extensive set of contacts across several subunits, that contribute to FliD oligomerization. We also demonstrate that the native C. jejuni flagellum filament is 11-stranded, contrary to a previously published cryo-EM structure, and propose a molecular model for the filament-cap interaction.
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Copyright, Publisher and Additional Information: | © The Author(s) 2020. 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/. | ||||||
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Institution: | The University of Sheffield | ||||||
Academic Units: | The University of Sheffield > Faculty of Science (Sheffield) > School of Biosciences (Sheffield) > Department of Molecular Biology and Biotechnology (Sheffield) | ||||||
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Depositing User: | Symplectic Sheffield | ||||||
Date Deposited: | 08 Jul 2020 15:26 | ||||||
Last Modified: | 08 Jul 2020 15:26 | ||||||
Status: | Published online | ||||||
Publisher: | Springer Science and Business Media LLC | ||||||
Refereed: | Yes | ||||||
Identification Number: | https://doi.org/10.1038/s41467-020-16981-4 | ||||||
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