|Entry||Database: EMDB / ID: EMD-0980|
|Title||CryoEM structure of S.typhimurium R-type straight flagellar filament made of FljB (A461V)|
|Biological species||Salmonella enterica subsp. enterica serovar Typhimurium (bacteria)|
|Method||single particle reconstruction / cryo EM / Resolution: 3.56 Å|
|Authors||Yamaguchi T / Toma S|
|Funding support|| Japan, 1 items |
|Citation||Journal: Biomolecules / Year: 2020|
Title: Structural and Functional Comparison of Flagellar Filaments Composed of FljB and FliC.
Authors: Tomoko Yamaguchi / Shoko Toma / Naoya Terahara / Tomoko Miyata / Masamichi Ashihara / Tohru Minamino / Keiichi Namba / Takayuki Kato /
Abstract: The bacterial flagellum is a motility organelle consisting of a long helical filament as a propeller and a rotary motor that drives rapid filament rotation to produce thrust. serovar Typhimurium has ...The bacterial flagellum is a motility organelle consisting of a long helical filament as a propeller and a rotary motor that drives rapid filament rotation to produce thrust. serovar Typhimurium has two genes of flagellin, and , for flagellar filament formation and autonomously switches their expression at a frequency of 10-10 per cell per generation. We report here differences in their structures and motility functions under high-viscosity conditions. A strain expressing FljB showed a higher motility than one expressing FliC under high viscosity. To examine the reasons for this motility difference, we carried out structural analyses of the FljB filament by electron cryomicroscopy and found that the structure was nearly identical to that of the FliC filament except for the position and orientation of the outermost domain D3 of flagellin. The density of domain D3 was much lower in FljB than FliC, suggesting that domain D3 of FljB is more flexible and mobile than that of FliC. These differences suggest that domain D3 plays an important role not only in changing antigenicity of the filament but also in optimizing motility function of the filament as a propeller under different conditions.
|Validation Report||Summary, Full report, XML, About validation report|
|Structure viewer||EM map: |
Downloads & links
|File||Download / File: emd_0980.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 1.06 Å|
|Symmetry||Space group: 1|
CCP4 map header:
|Projections & Slices|
-Half map: Cryo-EM half map 1 of 3D Refinement.
|Annotation||Cryo-EM half map 1 of 3D Refinement.|
|Projections & Slices|
-Half map: Cryo-EM half map 2 of 3D Refinement.
|Entire||Name: FljB / Details: R-type straight flagellar filament (A461V) / Number of components: 1|
-Component #1: protein, FljB
|Protein||Name: FljB / Details: R-type straight flagellar filament (A461V) / Recombinant expression: No|
|Source||Species: Salmonella enterica subsp. enterica serovar Typhimurium (bacteria)|
|Specimen||Specimen state: Filament / Method: cryo EM|
|Sample solution||pH: 7.8|
|Vitrification||Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 %|
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Imaging||Microscope: FEI TITAN KRIOS|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Electron dose: 10.3 e/Å2 / Illumination mode: OTHER|
|Lens||Magnification: 75000 X (nominal), 72273 X (calibrated) / Cs: 2.7 mm / Imaging mode: BRIGHT FIELD / Defocus: 500.0 - 2000.0 nm|
|Specimen Holder||Model: OTHER|
|Camera||Detector: FEI FALCON II (4k x 4k)|
|Image acquisition||Number of digital images: 2319|
|Processing||Method: single particle reconstruction / Applied symmetry: C1 (asymmetric) / Number of projections: 2319|
|3D reconstruction||Software: RELION / Resolution: 3.56 Å / Resolution method: FSC 0.143 CUT-OFF|
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