ArticleNature structural & molecular biology2019
Torque transmission mechanism of the curved bacterial flagellar hook revealed by cryo-EM.
Article in Nature structural & molecular biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed.
- Heterogeneity and multi-scale dynamics in the molecular bearing of the bacterial flagellum.Nature communications · 2026Article
- Ultraweak interactions drive cap-mediated positioning and elongation of the bacterial flagellar filament.Nature communications · 2025Article
- Curvature Generation and Engineering Principles fromACS nano · 2025Article
- The structure of the complete extracellular bacterial flagellum reveals the mechanism of flagellin incorporation.Nature microbiology · 2025Article
- In situ structure of a bacterial flagellar motor at subnanometre resolution reveals adaptations for increased torque.Nature microbiology · 2025Article
- FlgY, PflA, and PflB form a spoke-ring network in the high-torque flagellar motor ofProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Inhibitors of Lysinoalanine Cross-Linking in the Flagella Hook as Antimicrobials against Spirochetes.ACS chemical biology · 2025Article
- Cryo-EM reconstruction of helical polymers: Beyond the simple cases.Quarterly reviews of biophysics · 2024Review
- Structure and Dynamics of the Bacterial Flagellar Motor Complex.Biomolecules · 2024Review
- Molecular model of a bacterial flagellar motorbioRxiv : the preprint server for biology · 2024Article
- CryoEM reveals the structure of an archaeal pilus involved in twitching motility.Nature communications · 2024Article
- Helicobacter pylori FlgN binds its substrate FlgK and the flagellum ATPase FliI in a similar manner observed for the FliT chaperone.Protein science : a publication of the Protein Society · 2024Article
- Structure, Assembly, and Function of Flagella Responsible for Bacterial Locomotion.EcoSal Plus · 2023Review
- An overview of the structure and function of the flagellar hook FlgE protein.World journal of microbiology & biotechnology · 2023Review
- Article
- Helical ultrastructure of the metalloprotease meprin α in complex with a small molecule inhibitor.Nature communications · 2022Article
- Article
- Dynamic stiffening of the flagellar hook.Nature communications · 2022Article
- Structural basis for the helical filament formation of Escherichia coli glutamine synthetase.Protein science : a publication of the Protein Society · 2022Article
- An archaellum filament composed of two alternating subunits.Nature communications · 2022Article
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacterial locomotion by rotating flagella is achieved through the hook, which transmits torque from the motor to the filament. The hook is a tubular structure composed of a single type of protein, yet it adopts a curved shape. To perform its function, it must be simultaneously flexible and torsionally rigid. The molecular mechanism by which chemically identical subunits form such a dynamic structure is unknown. Here, we show the complete structure of the hook from Salmonella enterica in its supercoiled 'curved' state, at 2.9 Å resolution. Subunits in the curved hook are grouped into 11 distinctive conformations, each shared along 11 protofilaments. The domains of the elongated hook subunit behave as rigid bodies connected by two hinge regions. The reconstituted model demonstrates how identical subunits can dynamically change conformation by physical interactions while bending. These multiple subunit states contradict the two-state model, which is a key feature of flagellar polymorphism.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.