ArticleProceedings of the National Academy of Sciences of the United States of America2016
Insight into the flagella type III export revealed by the complex structure of the type III ATPase and its regulator.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 60 citations in OpenAlex.
- Article
- Uncoupling substrate delivery from export gate activation reveals distinct roles of the flagellar ATPase complex.Frontiers in microbiology · 2026Article
- The predicted sorting platform dynamically associates with the type III secretion system from Xanthomonas euvesicatoria in response to the external pH.BMC microbiology · 2025Article
- 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
- Molecular basis of the phenotypic variants arising from aMicrobial genomics · 2023Article
- Distinct Cytosolic Complexes Containing the Type III Secretion System ATPase Resolved by Three-Dimensional Single-Molecule Tracking in Live Yersinia enterocolitica.Microbiology spectrum · 2022Article
- Assembly and architecture of the type III secretion sorting platform.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Delineating specific regions of N- terminal domain of T3SS ATPase YsaN ofFrontiers in molecular biosciences · 2022Article
- Insight Into Distinct Functional Roles of the Flagellar ATPase Complex for Flagellar Assembly inFrontiers in microbiology · 2022Review
- Activation mechanism of the bacterial flagellar dual-fuel protein export engine.Biophysics and physicobiology · 2022Article
- Structure and Assembly of the Bacterial Flagellum.Sub-cellular biochemistry · 2022Review
- Membrane voltage-dependent activation mechanism of the bacterial flagellar protein export apparatus.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- A positive charge region of Salmonella FliI is required for ATPase formation and efficient flagellar protein export.Communications biology · 2021Article
- The FlgN chaperone activates the NaCommunications biology · 2021Article
- Protein Export via the Type III Secretion System of the Bacterial Flagellum.Biomolecules · 2021Review
- Architecture and Assembly of the Bacterial Flagellar Motor Complex.Sub-cellular biochemistry · 2021Review
- The PopN Gate-keeper Complex Acts on the ATPase PscN to Regulate the T3SS Secretion Switch from Early to Middle Substrates in Pseudomonas aeruginosa.Journal of molecular biology · 2020Article
- Structural Conservation and Adaptation of the Bacterial Flagella Motor.Biomolecules · 2020Review
- The Homologous Components of Flagellar Type III Protein Apparatus Have Acquired a Novel Function to Control Twitching Motility in a Non-Flagellated Biocontrol Bacterium.Biomolecules · 2020Article
- In Vitro Autonomous Construction of the Flagellar Axial Structure in Inverted Membrane Vesicles.Biomolecules · 2020Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
FliI and FliJ form the FliI6FliJ ATPase complex of the bacterial flagellar export apparatus, a member of the type III secretion system. The FliI6FliJ complex is structurally similar to the α3β3γ complex of F1-ATPase. The FliH homodimer binds to FliI to connect the ATPase complex to the flagellar base, but the details are unknown. Here we report the structure of the homodimer of a C-terminal fragment of FliH (FliHC2) in complex with FliI. FliHC2 shows an unusually asymmetric homodimeric structure that markedly resembles the peripheral stalk of the A/V-type ATPases. The FliHC2-FliI hexamer model reveals that the C-terminal domains of the FliI ATPase face the cell membrane in a way similar to the F/A/V-type ATPases. We discuss the mechanism of flagellar ATPase complex formation and a common origin shared by the type III secretion system and the F/A/V-type ATPases.
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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.