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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 | ||||||||||||||||||||||||
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![]() | MOTOR PROTEIN / Polar flagellum / Polar flagellar motor | ||||||||||||||||||||||||
Function / homology | ![]() 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 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 | ![]() | ||||||||||||||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.22 Å | ||||||||||||||||||||||||
![]() | Zhang, L. / Tan, J.X. / Zhou, Y. / Zhu, Y.Q. | ||||||||||||||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Cryo-EM structure of the polar flagellar motor-hook complex Authors: Zhang, L. / Tan, J.X. / Zhou, Y. / Zhu, Y.Q. | ||||||||||||||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 12.7 MB | Display | ![]() |
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PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 4.3 MB | Display | ![]() |
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Full document | ![]() | 5.3 MB | Display | |
Data in XML | ![]() | 1.6 MB | Display | |
Data in CIF | ![]() | 2.5 MB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 39790MC M: map data used to model this data C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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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) ![]() #6: Protein | Mass: 47434.438 Da / Num. of mol.: 40 / Source method: isolated from a natural source / Source: (natural) ![]() #7: Protein | Mass: 63915.605 Da / Num. of mol.: 72 / Source method: isolated from a natural source / Source: (natural) ![]() #8: Protein | Mass: 14239.950 Da / Num. of mol.: 5 / Source method: isolated from a natural source / Source: (natural) ![]() #11: Protein | Mass: 11135.679 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) ![]() #13: Protein | Mass: 42417.168 Da / Num. of mol.: 26 / Source method: isolated from a natural source / Source: (natural) ![]() #14: Protein | Mass: 27929.951 Da / Num. of mol.: 26 / Source method: isolated from a natural source / Source: (natural) ![]() #15: Protein | Mass: 16303.760 Da / Num. of mol.: 26 / Source method: isolated from a natural source / Source: (natural) ![]() #17: Protein | Mass: 37892.234 Da / Num. of mol.: 26 / Source method: isolated from a natural source / Source: (natural) ![]() #18: Protein | Mass: 33528.008 Da / Num. of mol.: 26 / Source method: isolated from a natural source / Source: (natural) ![]() #19: Protein | Mass: 24088.613 Da / Num. of mol.: 26 / Source method: isolated from a natural source / Source: (natural) ![]() |
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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) ![]() #3: Protein | Mass: 10329.615 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #4: Protein | | Mass: 28905.535 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #12: Protein | | Mass: 42197.297 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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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) ![]() #9: Protein | Mass: 14812.569 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) ![]() #10: Protein | Mass: 26987.387 Da / Num. of mol.: 5 / Source method: isolated from a natural source / Source: (natural) ![]() |
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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) ![]() #20: Protein/peptide | Mass: 1395.589 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #21: Protein/peptide | Mass: 1867.152 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Details
Has protein modification | Y |
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-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: all / Source: NATURAL |
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Molecular weight | Experimental value: NO |
Source (natural) | Organism: ![]() |
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: FEI TITAN KRIOS |
Electron gun | Electron source: ![]() |
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
EM software | Name: UCSF ChimeraX / Category: model fitting | |||||||||||||||
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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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