ArticleThe EMBO journal2002
Crystal structure of the middle and C-terminal domains of the flagellar rotor protein FliG.
Article in The EMBO journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.
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Who cites it
74 citing papers in PubMed.
- 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
- CryoEM structures reveal how the bacterial flagellum rotates and switches direction.Nature microbiology · 2024Article
- Changes in the hydrophobic network of the FliGiScience · 2023Article
- Flagellar brake protein YcgR interacts with motor proteins MotA and FliG to regulate the flagellar rotation speed and direction.Frontiers in microbiology · 2023Article
- Novel transient cytoplasmic rings stabilize assembling bacterial flagellar motors.The EMBO journal · 2022Article
- Bridging the N-terminal and middle domains in FliG of the flagellar rotor.Current research in structural biology · 2022Article
- Structural Conservation and Adaptation of the Bacterial Flagella Motor.Biomolecules · 2020Review
- The flagellar motor ofeLife · 2020Article
- The Architectural Dynamics of the Bacterial Flagellar Motor Switch.Biomolecules · 2020Review
- New Twists and Turns in Bacterial Locomotion and Signal Transduction.Journal of bacteriology · 2019Review
- Organization of the Flagellar Switch Complex of Bacillus subtilis.Journal of bacteriology · 2019Article
- Directional Switching Mechanism of the Bacterial Flagellar Motor.Computational and structural biotechnology journal · 2019Review
- Rotational direction of flagellar motor from the conformation of FliG middle domain in marine Vibrio.Scientific reports · 2018Article
- Three SpoA-domain proteins interact in the creation of the flagellar type III secretion system inThe Journal of biological chemistry · 2018Article
- The role of conserved charged residues in the bidirectional rotation of the bacterial flagellar motor.MicrobiologyOpen · 2018Article
- Architecture of the Flagellar Switch Complex of Escherichia coli: Conformational Plasticity of FliG and Implications for Adaptive Remodeling.Journal of molecular biology · 2017Article
- Co-Folding of a FliF-FliG Split Domain Forms the Basis of the MS:C Ring Interface within the Bacterial Flagellar Motor.Structure (London, England : 1993) · 2017Article
- The Limiting Speed of the Bacterial Flagellar Motor.Biophysical journal · 2016Article
- The Gearbox of the Bacterial Flagellar Motor Switch.Structure (London, England : 1993) · 2016Article
14 more citing papers are in PubMed but not listed here.
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3 authors.
Funding
Abstract
The FliG protein is essential for assembly, rotation and clockwise/counter-clockwise (CW/CCW) switching of the bacterial flagellum. About 25 copies of FliG are present in a large rotor-mounted assembly termed the 'switch complex', which also contains the proteins FliM and FliN. Mutational studies have identified the segments of FliG most crucial for flagellar assembly, rotation and switching. The structure of the C-terminal domain, which functions specifically in rotation, was reported previously. Here, we describe the crystal structure of a larger fragment of the FliG protein from Thermotoga maritima, which encompasses the middle and C-terminal parts of the protein (termed FliG-MC). The FliG-MC molecule consists of two compact globular domains, linked by an alpha-helix and an extended segment that contains a well-conserved Gly-Gly motif. Mutational studies indicate that FliM binds to both of the globular domains, and given the flexibility of the linking segment, FliM is likely to determine the relative orientation of the domains in the flagellum. We propose a model for the organization of FliG-MC molecules in the flagellum, and suggest that CW/CCW switching might occur by movement of the C-terminal domain relative to other parts of FliG, under the control of FliM.
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