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Yorodumi- EMDB-70016: Focus-refined structures of FlgY spokes in the Helicobacter pylor... -
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Open data
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Basic information
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| Title | Focus-refined structures of FlgY spokes in the Helicobacter pylori flagellar motor in situ | |||||||||
Map data | Focus-refined structures of FlgY spokes in the Helicobacter pylori flagellar motor | |||||||||
Sample |
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Keywords | H. pylori / Flagella / Complex / Flagellar motor / MOTOR PROTEIN | |||||||||
| Biological species | Helicobacter pylori G27 (bacteria) | |||||||||
| Method | subtomogram averaging / cryo EM / Resolution: 10.5 Å | |||||||||
Authors | Tachiyama S / Liu J | |||||||||
| Funding support | United States, 2 items
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Citation | Journal: Proc Natl Acad Sci U S A / Year: 2025Title: FlgY, PflA, and PflB form a spoke-ring network in the high-torque flagellar motor of . Authors: Shoichi Tachiyama / Kyle Rosinke / Mohammad F Khan / Xiaotian Zhou / Yue Xin / Jack M Botting / Jian Yue / Anna Roujeinikova / Timothy R Hoover / Jun Liu / ![]() Abstract: has evolved distinct flagellar motility to colonize the human stomach. Rotation of the flagella is driven by one of the largest known bacterial flagellar motors. In addition to the core motor ... has evolved distinct flagellar motility to colonize the human stomach. Rotation of the flagella is driven by one of the largest known bacterial flagellar motors. In addition to the core motor components found in and , the flagellar motor in possesses many accessories that enable the bacteria to penetrate the gastric mucus layer. Here, we utilize cryoelectron tomography with molecular genetics and biochemical approaches to characterize three accessory proteins, FlgY, PflA, and PflB, and their roles in flagellar assembly and motility. Comparative analyses of in situ flagellar motor structures from , , and mutants and wild-type reveal that FlgY forms a 13-fold proximal spoke-ring around the MS-ring and that PflA and PflB form an 18-fold distal spoke-ring enclosing 18 torque-generating stator complexes. We build a pseudoatomic model of the motor by leveraging AlphaFold-predicted structures, protein-protein interactions, and motor structures. Our model suggests that the FlgY spoke-ring functions as a bearing around the rotating MS-ring and as a template for stabilizing the PflA-PflB spoke-ring, thus enabling the recruitment of 18 stator complexes for high-torque generation. Overall, our study sheds light on how this spoke-ring network between the MS-ring and stator complexes enables the unique motility of . As these accessory proteins are conserved in the phylum Campylobacterota, our findings apply broadly to a better understanding of how polar flagella help bacteria thrive in gastric and enteric niches. | |||||||||
| History |
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_70016.map.gz | 37.6 MB | EMDB map data format | |
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| Header (meta data) | emd-70016-v30.xml emd-70016.xml | 14.3 KB 14.3 KB | Display Display | EMDB header |
| Images | emd_70016.png | 723 KB | ||
| Filedesc metadata | emd-70016.cif.gz | 4.3 KB | ||
| Others | emd_70016_half_map_1.map.gz emd_70016_half_map_2.map.gz | 37.6 MB 37.6 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-70016 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-70016 | HTTPS FTP |
-Validation report
| Summary document | emd_70016_validation.pdf.gz | 1.5 MB | Display | EMDB validaton report |
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| Full document | emd_70016_full_validation.pdf.gz | 1.5 MB | Display | |
| Data in XML | emd_70016_validation.xml.gz | 11 KB | Display | |
| Data in CIF | emd_70016_validation.cif.gz | 13.4 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-70016 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-70016 | HTTPS FTP |
-Related structure data
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_70016.map.gz / Format: CCP4 / Size: 40.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | Focus-refined structures of FlgY spokes in the Helicobacter pylori flagellar motor | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 2.148 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: Half map of focus-refined structures of FlgY spokes...
| File | emd_70016_half_map_1.map | ||||||||||||
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| Annotation | Half map of focus-refined structures of FlgY spokes in the Helicobacter pylori flagellar motor | ||||||||||||
| Projections & Slices |
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| Density Histograms |
-Half map: Half map of focus-refined structures of FlgY spokes...
| File | emd_70016_half_map_2.map | ||||||||||||
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| Annotation | Half map of focus-refined structures of FlgY spokes in the Helicobacter pylori flagellar motor | ||||||||||||
| Projections & Slices |
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| Density Histograms |
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Sample components
-Entire : Helicobacter pylori
| Entire | Name: ![]() |
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| Components |
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-Supramolecule #1: Helicobacter pylori
| Supramolecule | Name: Helicobacter pylori / type: cell / ID: 1 / Parent: 0 |
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| Source (natural) | Organism: Helicobacter pylori G27 (bacteria) |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | subtomogram averaging |
| Aggregation state | cell |
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Sample preparation
| Buffer | pH: 7.4 |
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| Vitrification | Cryogen name: ETHANE-PROPANE |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Specialist optics | Energy filter - Name: GIF Bioquantum / Energy filter - Slit width: 20 eV |
| Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 1.96 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 5.0 µm / Nominal defocus min: 3.0 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
| Final reconstruction | Applied symmetry - Point group: C13 (13 fold cyclic) / Resolution.type: BY AUTHOR / Resolution: 10.5 Å / Resolution method: FSC 0.5 CUT-OFF / Number subtomograms used: 9638 |
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| Extraction | Number tomograms: 567 / Number images used: 1635 |
| CTF correction | Type: PHASE FLIPPING ONLY |
| Final angle assignment | Type: OTHER |
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About Yorodumi



Keywords
Helicobacter pylori G27 (bacteria)
Authors
United States, 2 items
Citation

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FIELD EMISSION GUN
