ArticleScientific reports2016
Structural flexibility of the periplasmic protein, FlgA, regulates flagellar P-ring assembly in Salmonella enterica.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 18 citations in OpenAlex.
- The last bacterial common ancestor encoded a complex flagellum.bioRxiv : the preprint server for biology · 2026Article
- Exploring the conformational landscape of adenylate kinase and beyond with protein folding models.Scientific reports · 2026Article
- Electron Cryo-Tomography Reveals thebioRxiv : the preprint server for biology · 2025Article
- Volatile Organic Compounds from Pseudomonas koreensis KF32 and P. fitomaticsae KF45 Suppress Ralstonia pseudosolanacearum and Reduce Bacterial Wilt in Tomato.The plant pathology journal · 2025Article
- A flagella-dependentmBio · 2025Article
- Structure and Dynamics of the Bacterial Flagellar Motor Complex.Biomolecules · 2024Review
- Structure, Assembly, and Function of Flagella Responsible for Bacterial Locomotion.EcoSal Plus · 2023Review
- The Missing Pieces: The Role of Secretion Systems inBiomolecules · 2023Review
- Structure of the molecular bushing of the bacterial flagellar motor.Nature communications · 2021Article
- Review
- Structural Conservation and Adaptation of the Bacterial Flagella Motor.Biomolecules · 2020Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A periplasmic flagellar chaperone protein, FlgA, is required for P-ring assembly in bacterial flagella of taxa such as Salmonella enterica or Escherichia coli. The mechanism of chaperone-mediated P-ring formation is poorly understood. Here we present the open and closed crystal structures of FlgA from Salmonella enterica serovar Typhimurium, grown under different crystallization conditions. An intramolecular disulfide cross-linked form of FlgA caused a dominant negative effect on motility of the wild-type strain. Pull-down experiments support a specific protein-protein interaction between FlgI, the P-ring component protein, and the C-terminal domain of FlgA. Surface plasmon resonance and limited-proteolysis indicate that flexibility of the domain is reduced in the covalently closed form. These results show that the structural flexibility of the C-terminal domain of FlgA, which is related to the structural difference between the two crystal forms, is intrinsically associated with its molecular chaperone function in P-ring assembly.
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Registered trials
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