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Open data
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Basic information
| Entry | Database: PDB / ID: 8z60 | |||||||||||||||||||||||||||
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| Title | Cryo-EM structure of the polar flagellar motor-hook complex | |||||||||||||||||||||||||||
Components |
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Keywords | MOTOR PROTEIN / Polar flagellum / Polar flagellar motor | |||||||||||||||||||||||||||
| Function / homology | Function and homology informationbacterial-type flagellum basal body, distal rod / bacterial-type flagellum basal body, rod / bacterial-type flagellum organization / bacterial-type flagellum hook / bacterial-type flagellum basal body, MS ring / bacterial-type flagellum basal body / bacterial-type flagellum-dependent swarming motility / cytoskeletal motor activity / bacterial-type flagellum assembly / protein secretion ...bacterial-type flagellum basal body, distal rod / bacterial-type flagellum basal body, rod / bacterial-type flagellum organization / bacterial-type flagellum hook / bacterial-type flagellum basal body, MS ring / bacterial-type flagellum basal body / bacterial-type flagellum-dependent swarming motility / cytoskeletal motor activity / bacterial-type flagellum assembly / protein secretion / bacterial-type flagellum-dependent cell motility / protein targeting / cell outer membrane / structural molecule activity / plasma membrane / cytosol Similarity search - Function | |||||||||||||||||||||||||||
| Biological species | Vibrio alginolyticus (bacteria) | |||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.22 Å | |||||||||||||||||||||||||||
Authors | Zhang, L. / Tan, J.X. / Zhou, Y. / Zhu, Y.Q. | |||||||||||||||||||||||||||
| Funding support | China, 3items
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Citation | Journal: Protein Cell / Year: 2026Title: Molecular basis of high-torque transmission of the Vibrio polar flagellar motor. Authors: Ling Zhang / Jiaxing Tan / Xuemin Duan / Xiaofei Wang / Ting Wang / Keke Yuan / Michio Homma / Seiji Kojima / Yan Zhou / Yongqun Zhu / ![]() Abstract: The bacterial flagellar motor is a protein nanomachine that rotates the flagellum to facilitate bacterial motility. These motors exhibit structural diversity among species, enabling the transmission ...The bacterial flagellar motor is a protein nanomachine that rotates the flagellum to facilitate bacterial motility. These motors exhibit structural diversity among species, enabling the transmission of varying torques to flagellar filaments to grant bacteria diverse swimming capabilities. Compared to peritrichous flagellar motors, polar flagellar motors are faster machines that transmit higher torque to drive high-speed motility in liquids and empower swimming in viscous environments. However, structural basis of high-torque transmission of the polar flagellar motors is still unclear. Here we present a cryo-electron microscopy structure of the polar flagellar motor in complex with the hook from Vibrio alginolyticus, comprising 295 subunits from 18 proteins. Compared to the peritrichous flagellar rod, this structure reveals an increased number of inter-subunit interactions in the rod of the polar flagellar motor. Nine phospholipid molecules insert into the interface between the export apparatus and the proximal rod. The LP ring contains more electrostatic charges on the inner surface and has fewer physical contacts with the rod, while the HT ring tightly binds to the outer surface of the LP ring. FlrP, a protein of previously unknown function, is identified as a new component of the polar flagellar motor, and extensively participates in the interactions of 15 FliF peptides of the MS ring with the rod. In contrast to that in the peritrichous flagellum, the hook in the polar flagellum has two different conformational states, L- and R-types. These findings provide unprecedented insights into structural adaptations of the bacterial polar flagellar motors for high-torque transmission. | |||||||||||||||||||||||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 8z60.cif.gz | 12.8 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb8z60.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 8z60.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/z6/8z60 ftp://data.pdbj.org/pub/pdb/validation_reports/z6/8z60 | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 39790MC ![]() 8z5nC ![]() 8z5sC ![]() 8z5uC ![]() 8z5vC ![]() 8z5wC ![]() 8z5xC ![]() 8z5yC ![]() 8z5zC M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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Components
-Protein , 11 types, 281 molecules 09A1A2A3AbAcAdAeAfAgAhAiAjAkAlAmAnAoApAqArAsAtAuAvAwAxAyAz...
| #1: Protein | Mass: 21518.053 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Vibrio alginolyticus (bacteria) / Strain: KK148#6: Protein | Mass: 47434.438 Da / Num. of mol.: 40 / Source method: isolated from a natural source / Source: (natural) Vibrio alginolyticus (bacteria) / Strain: KK148 / References: UniProt: A0A0H0YA78#7: Protein | Mass: 63915.605 Da / Num. of mol.: 72 / Source method: isolated from a natural source / Source: (natural) Vibrio alginolyticus (bacteria) / Strain: KK148 / References: UniProt: Q75N27#8: Protein | Mass: 14239.950 Da / Num. of mol.: 5 / Source method: isolated from a natural source / Source: (natural) Vibrio alginolyticus (bacteria) / Strain: KK148 / References: UniProt: A0A0G9LZG6#11: Protein | Mass: 11135.679 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) Vibrio alginolyticus (bacteria) / Strain: KK148 / References: UniProt: A0A0H0Y9C1#13: Protein | Mass: 42417.168 Da / Num. of mol.: 26 / Source method: isolated from a natural source / Source: (natural) Vibrio alginolyticus (bacteria) / Strain: KK148 / References: UniProt: D9N551#14: Protein | Mass: 27929.951 Da / Num. of mol.: 26 / Source method: isolated from a natural source / Source: (natural) Vibrio alginolyticus (bacteria) / Strain: KK148#15: Protein | Mass: 16303.760 Da / Num. of mol.: 26 / Source method: isolated from a natural source / Source: (natural) Vibrio alginolyticus (bacteria) / Strain: KK148 / References: UniProt: A0A0H0Y943#17: Protein | Mass: 37892.234 Da / Num. of mol.: 26 / Source method: isolated from a natural source / Source: (natural) Vibrio alginolyticus (bacteria) / Strain: KK148#18: Protein | Mass: 33528.008 Da / Num. of mol.: 26 / Source method: isolated from a natural source / Source: (natural) Vibrio alginolyticus (bacteria) / Strain: KK148 / References: UniProt: P74944#19: Protein | Mass: 24088.613 Da / Num. of mol.: 26 / Source method: isolated from a natural source / Source: (natural) Vibrio alginolyticus (bacteria) / Strain: KK148 / References: UniProt: Q93R25 |
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-Flagellar biosynthetic protein ... , 4 types, 11 molecules 123yz45678x
| #2: Protein | Mass: 31314.904 Da / Num. of mol.: 5 / Source method: isolated from a natural source / Source: (natural) Vibrio alginolyticus (bacteria) / Strain: KK148 / References: UniProt: A0A1W6TTE6#3: Protein | Mass: 10329.615 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Vibrio alginolyticus (bacteria) / Strain: KK148 / References: UniProt: A0A0H0YAF4#4: Protein | | Mass: 28905.535 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Vibrio alginolyticus (bacteria) / Strain: KK148 / References: UniProt: A0A0H0YFV7#12: Protein | | Mass: 42197.297 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Vibrio alginolyticus (bacteria) / Strain: KK148 / References: UniProt: A0A0H0YB55 |
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-Flagellar basal-body rod protein ... , 3 types, 38 molecules AAPAQARASATAUAVAWAXAYAZAaBCPQRSTUVWXYZaghi...
| #5: Protein | Mass: 27908.943 Da / Num. of mol.: 27 / Source method: isolated from a natural source / Source: (natural) Vibrio alginolyticus (bacteria) / Strain: KK148 / References: UniProt: A0A0H0YB44#9: Protein | Mass: 14812.569 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) Vibrio alginolyticus (bacteria) / Strain: KK148 / References: UniProt: A0A0G9LZH2#10: Protein | Mass: 26987.387 Da / Num. of mol.: 5 / Source method: isolated from a natural source / Source: (natural) Vibrio alginolyticus (bacteria) / Strain: KK148 / References: UniProt: A0A0G9M4M9 |
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-Protein/peptide , 3 types, 37 molecules B0CECHA6CMCRCWCbCgClCqCvC1C6B4BABFBKBPBUBZBeBjBoBtByD0D6D7D8...
| #16: Protein/peptide | Mass: 1450.630 Da / Num. of mol.: 27 / Fragment: The N-terminus / Source method: isolated from a natural source / Source: (natural) Vibrio alginolyticus (bacteria) / Strain: KK148#20: Protein/peptide | Mass: 1395.589 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Vibrio alginolyticus (bacteria) / Strain: KK148#21: Protein/peptide | Mass: 1867.152 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) Vibrio alginolyticus (bacteria) / Strain: KK148 |
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-Non-polymers , 2 types, 9 molecules 


| #22: Chemical | ChemComp-PGT / ( #23: Chemical | ChemComp-XKP / ( |
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-Details
| Has ligand of interest | Y |
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| Has protein modification | Y |
-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
| Component | Name: The polar flagellar motor-hook complex / Type: COMPLEX / Entity ID: #1-#21 / Source: NATURAL |
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| Molecular weight | Experimental value: NO |
| Source (natural) | Organism: Vibrio alginolyticus (bacteria) / Strain: KK148 |
| Buffer solution | pH: 8 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Specimen support | Grid material: COPPER / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R1.2/1.3 |
| Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277.15 K |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: TFS KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal magnification: 105000 X / Nominal defocus max: 1800 nm / Nominal defocus min: 1200 nm |
| Image recording | Electron dose: 50 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k) |
| EM imaging optics | Energyfilter name: TFS Selectris / Energyfilter slit width: 10 eV |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| Particle selection | Num. of particles selected: 329955 | ||||||||||||||||||||||||
| Symmetry | Point symmetry: C100 (100 fold cyclic) | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3.22 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 61395 / Symmetry type: POINT | ||||||||||||||||||||||||
| Atomic model building | Protocol: OTHER | ||||||||||||||||||||||||
| Atomic model building |
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About Yorodumi




Vibrio alginolyticus (bacteria)
China, 3items
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FIELD EMISSION GUN