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Open data
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Basic information
| Entry | ![]() | |||||||||
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| Title | Structure of flagellin FlaB filament in H. pylori | |||||||||
Map data | Flagellin FlaB filament in H. pylori | |||||||||
Sample |
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Keywords | Flagella / Flagellin / Filament / STRUCTURAL PROTEIN | |||||||||
| Function / homology | Function and homology informationbacterial-type flagellum / structural molecule activity / extracellular region Similarity search - Function | |||||||||
| Biological species | ![]() Helicobacter pylori B128 (bacteria) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.22 Å | |||||||||
Authors | Kumar R / Yu H / Tachiyama S / Liu J | |||||||||
| Funding support | United States, 1 items
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Citation | Journal: PNAS Nexus / Year: 2026Title: Assembly and glycosylation of sheathed flagella. Authors: Rajeev Kumar / Shoichi Tachiyama / Huaxin Yu / Samira Heydari / Jiaqi Guo / Jack M Botting / Wangbiao Guo / Timothy R Hoover / Jun Liu / ![]() Abstract: The bacterial flagellum is a complex nanomachine essential for motility, colonization, and invasion in diverse species. has evolved elaborate sheathed flagella that enable migration through the ...The bacterial flagellum is a complex nanomachine essential for motility, colonization, and invasion in diverse species. has evolved elaborate sheathed flagella that enable migration through the highly viscous gastric mucus layer to reach its colonization niche on the gastric epithelium, yet the molecular basis for these unique adaptations has remained elusive. Here, we use in situ single-particle cryo-electron microscopy to determine near-atomic structures of the flagellar filament within the membranous sheath of . The major flagellin FlaA constitutes the bulk of the filament, whereas the minor flagellin FlaB contributes critically to the hook-proximal region. Both FlaA and FlaB form a conserved core surrounded by variable surface-exposed domains. Our structures further reveal that pseudaminic acid glycans decorate these domains, where they mediate inter- and intra-subunit contacts that stabilize the filament and confer a negatively charged surface. Together, these findings support a model in which the filament rotates independently of the membranous sheath to drive motility and provide a molecular framework for understanding how the sheathed flagellum enables colonization and persistence within the gastric niche. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_72948.map.gz | 322.1 MB | EMDB map data format | |
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| Header (meta data) | emd-72948-v30.xml emd-72948.xml | 16 KB 16 KB | Display Display | EMDB header |
| Images | emd_72948.png | 97.5 KB | ||
| Filedesc metadata | emd-72948.cif.gz | 5.5 KB | ||
| Others | emd_72948_half_map_1.map.gz emd_72948_half_map_2.map.gz | 318.4 MB 318.4 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-72948 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-72948 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9yh1MC ![]() 9yguC M: atomic model generated by this map C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_72948.map.gz / Format: CCP4 / Size: 343 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | Flagellin FlaB filament in H. pylori | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.068 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: FlaB Half map B
| File | emd_72948_half_map_1.map | ||||||||||||
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| Annotation | FlaB Half map B | ||||||||||||
| Projections & Slices |
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| Density Histograms |
-Half map: FlaB Half map A
| File | emd_72948_half_map_2.map | ||||||||||||
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| Annotation | FlaB Half map A | ||||||||||||
| Projections & Slices |
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| Density Histograms |
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Sample components
-Entire : Flagellar filament composed of flagellin FlaB
| Entire | Name: Flagellar filament composed of flagellin FlaB |
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| Components |
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-Supramolecule #1: Flagellar filament composed of flagellin FlaB
| Supramolecule | Name: Flagellar filament composed of flagellin FlaB / type: cell / ID: 1 / Parent: 0 / Macromolecule list: #1 |
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| Source (natural) | Organism: ![]() |
-Macromolecule #1: Flagellin
| Macromolecule | Name: Flagellin / type: protein_or_peptide / ID: 1 / Number of copies: 33 / Enantiomer: LEVO |
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| Source (natural) | Organism: Helicobacter pylori B128 (bacteria) |
| Molecular weight | Theoretical: 53.88966 KDa |
| Sequence | String: SFRINTNIAA LTSHAVGVQN NRDLSSSLEK LSSGLRINKA ADDSSGMAIA DSLRSQSANL GQAIRNANDA IGMVQTADKA MDEQIKILD TIKTKAVQAA QDGQTLESRR ALQSDIQRLL EELDNIANTT SFNGQQMLSG SFSNKEFQIG AYSNTTVKAS I GSTSSDKI ...String: SFRINTNIAA LTSHAVGVQN NRDLSSSLEK LSSGLRINKA ADDSSGMAIA DSLRSQSANL GQAIRNANDA IGMVQTADKA MDEQIKILD TIKTKAVQAA QDGQTLESRR ALQSDIQRLL EELDNIANTT SFNGQQMLSG SFSNKEFQIG AYSNTTVKAS I GSTSSDKI GHVRMETSSF SGEGMLASAA AQNLTEVGLN FKQVNGVNDY KIETVRISTS AGTGIGALSE IINRFSNTLG VR ASYNVMA TGGTPVQSGT VRELTINGVE IGTVNDVHKN DADGRLTNAI NSVKDRTGVE ASLDIQGRIN LHSIDGRAIS VHA ASASGQ VFGGGNFAGI SGTQHAVIGR LTLTRTDARD IIVSGVNFSH VGFHSAQGVA EYTVNLRAVR GIFDANVASA AGAN ANGAQ AETNSQGIGA GVTSLKGAMI VMDMADSART QLDKIRSDMG SVQMELVTTI NNISVTQVNV KAAESQIRDV DFAEE SANF SKYNILAQSG SFAMAQANAV QQNVLRLLQ UniProtKB: Flagellin |
-Macromolecule #2: 5,7-diamino-3,5,7,9-tetradeoxy-L-glycero-alpha-L-manno-non-2-ulop...
| Macromolecule | Name: 5,7-diamino-3,5,7,9-tetradeoxy-L-glycero-alpha-L-manno-non-2-ulopyranosonic acid type: ligand / ID: 2 / Number of copies: 297 / Formula: P8E |
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| Molecular weight | Theoretical: 250.249 Da |
| Chemical component information | ![]() ChemComp-P8E: |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | filament |
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Sample preparation
| Buffer | pH: 7 |
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| Vitrification | Cryogen name: ETHANE-PROPANE |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | Film or detector model: GATAN K2 BASE (4k x 4k) / Average electron dose: 70.0 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: 2.0 µm / Nominal defocus min: 1.0 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Keywords
Authors
United States, 1 items
Citation


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Processing
FIELD EMISSION GUN
