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Yorodumi- PDB-8t8o: CCW Flagellar Switch Complex - FliF, FliG, FliM, and FliN forming... -
+Open data
-Basic information
Entry | Database: PDB / ID: 8t8o | ||||||
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Title | CCW Flagellar Switch Complex - FliF, FliG, FliM, and FliN forming 34-mer C-ring from Salmonella | ||||||
Components |
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Keywords | MOTOR PROTEIN / Domain Swap / Symmetry mismatch / Flagellar component / Switch complex | ||||||
Function / homology | Function and homology information bacterial-type flagellum basal body, MS ring / bacterial-type flagellum basal body / cytoskeletal motor activity / bacterial-type flagellum-dependent cell motility / chemotaxis / plasma membrane Similarity search - Function | ||||||
Biological species | Salmonella enterica subsp. enterica serovar Typhimurium (bacteria) | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4 Å | ||||||
Authors | Singh, P.K. / Iverson, T.M. | ||||||
Funding support | United States, 1items
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Citation | Journal: To Be Published Title: Structural basis for directional rotation of the Salmonella flagellum Authors: Singh, P.K. / Iverson, T.M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 8t8o.cif.gz | 4.7 MB | Display | PDBx/mmCIF format |
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PDB format | pdb8t8o.ent.gz | Display | PDB format | |
PDBx/mmJSON format | 8t8o.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/t8/8t8o ftp://data.pdbj.org/pub/pdb/validation_reports/t8/8t8o | HTTPS FTP |
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-Related structure data
Related structure data | 41100MC 8t8pC M: map data used to model this data C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
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1 |
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-Components
#1: Protein/peptide | Mass: 5644.328 Da / Num. of mol.: 34 / Fragment: C-terminal domain (UNP residues 514-560) Source method: isolated from a genetically manipulated source Source: (gene. exp.) Salmonella enterica subsp. enterica serovar Typhimurium (bacteria) Gene: fliF, fla AII.1, fla BI, STM1969 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P15928 #2: Protein | Mass: 36890.957 Da / Num. of mol.: 34 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Salmonella enterica subsp. enterica serovar Typhimurium (bacteria) Gene: fliG / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: A0A0F7J9E2 #3: Protein | Mass: 33758.836 Da / Num. of mol.: 34 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Salmonella enterica subsp. enterica serovar Typhimurium (bacteria) Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: A0A0D6FLG5 #4: Protein | Mass: 14801.823 Da / Num. of mol.: 102 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Salmonella enterica subsp. enterica serovar Typhimurium (bacteria) Gene: fliN / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: A0A0D6FLI0 |
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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 |
-Sample preparation
Component | Name: Flagellar MS-ring and C-ring complex 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: Salmonella enterica subsp. enterica serovar Typhimurium (bacteria) |
Source (recombinant) | Organism: Escherichia coli BL21(DE3) (bacteria) |
Buffer solution | pH: 7.5 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE |
-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: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
Electron lens | Mode: BRIGHT FIELDBright-field microscopy / Nominal defocus max: 2000 nm / Nominal defocus min: 1000 nm |
Image recording | Electron dose: 51.557 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
-Processing
EM software |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
Symmetry | Point symmetry: C34 (34 fold cyclic) | ||||||||||||||||||||||||
3D reconstruction | Resolution: 4 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 51268 / Symmetry type: POINT | ||||||||||||||||||||||||
Refine LS restraints |
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