ArticleNature structural & molecular biology2016
Domain-swap polymerization drives the self-assembly of the bacterial flagellar motor.
Article in Nature structural & molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 55 citations in OpenAlex.
- Structural insights into the assembly and evolution of a complex bacterial flagellar motor.Nature microbiology · 2026Article
- Regulatory Role of a Hydrophobic Core in the FliG C-Terminal Domain in the Rotary Direction of a Flagellar Motor.Biomolecules · 2025Article
- Structure and Dynamics of the Bacterial Flagellar Motor Complex.Biomolecules · 2024Review
- Hybrid Exb/Mot stators require substitutions distant from the chimeric pore to power flagellar rotation.Journal of bacteriology · 2024Article
- Structural basis of directional switching by the bacterial flagellum.Nature microbiology · 2024Article
- Structure, Assembly, and Function of Flagella Responsible for Bacterial Locomotion.EcoSal Plus · 2023Review
- Structural Basis of Directional Switching by the Bacterial Flagellum.Research square · 2023Article
- Changes in the hydrophobic network of the FliGiScience · 2023Article
- Article
- Modeling Bacterial Flagellar Motor With New Structure Information: Rotational Dynamics of Two Interacting Protein Nano-Rings.Frontiers in microbiology · 2022Article
- Bridging the N-terminal and middle domains in FliG of the flagellar rotor.Current research in structural biology · 2022Article
- Single-molecule optical tweezers reveals folding steps of the domain swapping mechanism of a protein.Biophysical journal · 2021Article
- Native flagellar MS ring is formed by 34 subunits with 23-fold and 11-fold subsymmetries.Nature communications · 2021Article
- Architecture and Assembly of the Bacterial Flagellar Motor Complex.Sub-cellular biochemistry · 2021Review
- The flagellar motor ofeLife · 2020Article
- Small molecule AX-024 reduces T cell proliferation independently of CD3ϵ/Nck1 interaction, which is governed by a domain swap in the Nck1-SH3.1 domain.The Journal of biological chemistry · 2020Article
- The Architectural Dynamics of the Bacterial Flagellar Motor Switch.Biomolecules · 2020Review
- Article
- Flagella-Driven Motility of Bacteria.Biomolecules · 2019Review
- Organization of the Flagellar Switch Complex of Bacillus subtilis.Journal of bacteriology · 2019Article
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Authors and funding
17 authors at 4 institutions in 4 countries.
Funding
Abstract
Large protein complexes assemble spontaneously, yet their subunits do not prematurely form unwanted aggregates. This paradox is epitomized in the bacterial flagellar motor, a sophisticated rotary motor and sensory switch consisting of hundreds of subunits. Here we demonstrate that Escherichia coli FliG, one of the earliest-assembling flagellar motor proteins, forms ordered ring structures via domain-swap polymerization, which in other proteins has been associated with uncontrolled and deleterious protein aggregation. Solution structural data, in combination with in vivo biochemical cross-linking experiments and evolutionary covariance analysis, revealed that FliG exists predominantly as a monomer in solution but only as domain-swapped polymers in assembled flagellar motors. We propose a general structural and thermodynamic model for self-assembly, in which a structural template controls assembly and shapes polymer formation into rings.
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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.