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- PDB-8vkq: CW Flagellar Switch Complex - FliF, FliG, FliM, and FliN forming ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 8vkq | ||||||
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Title | CW Flagellar Switch Complex - FliF, FliG, FliM, and FliN forming the C-ring from Salmonella | ||||||
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![]() | MOTOR PROTEIN / Domain Swap / Symmetry mismatch / Flagellar component / Switch complex | ||||||
Function / homology | ![]() bacterial-type flagellum basal body, MS ring / bacterial-type flagellum basal body / bacterial-type flagellum-dependent swarming motility / positive chemotaxis / cytoskeletal motor activity / bacterial-type flagellum-dependent cell motility / chemotaxis / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.6 Å | ||||||
![]() | Singh, P.K. / Iverson, T.M. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Structural basis for rotation and directional switching by the combined MS- and C-rings of bacterial flagella. Authors: Singh, P.K. / Iverson, T.M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 4.3 MB | Display | ![]() |
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PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 2 MB | Display | ![]() |
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Full document | ![]() | 2.2 MB | Display | |
Data in XML | ![]() | 556 KB | Display | |
Data in CIF | ![]() | 960.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 43327MC ![]() 8vibC ![]() 8vidC ![]() 8vkrC 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
#1: Protein | Mass: 61295.645 Da / Num. of mol.: 34 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: fliF, fla AII.1, fla BI, STM1969 / Production host: ![]() ![]() #2: Protein | Mass: 36860.930 Da / Num. of mol.: 34 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: fliG, AUA10_01480, AUA59_00550 / Production host: ![]() ![]() #3: Protein | Mass: 32992.895 Da / Num. of mol.: 34 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: fliM, G0L96_06560 / Production host: ![]() ![]() #4: Protein | Mass: 14801.823 Da / Num. of mol.: 102 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: fliN, flaN, motD, STM1977 / Production host: ![]() ![]() |
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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: Flagellar C-ring containing FliF, FliG, FliM, and FliN Type: COMPLEX / Entity ID: all / Source: RECOMBINANT |
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Molecular weight | Value: 3.5 MDa / Experimental value: NO |
Source (natural) | Organism: ![]() |
Source (recombinant) | Organism: ![]() ![]() |
Buffer solution | pH: 7.5 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE |
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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 defocus max: 2000 nm / Nominal defocus min: 1000 nm |
Image recording | Electron dose: 56.323 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
EM software |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | |||||||||||||||||||||||||||||||||||
3D reconstruction | Resolution: 4.6 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 7201 / Symmetry type: POINT |