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Open data
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Basic information
| Entry | Database: PDB / ID: 9yec | ||||||||||||||||||||||||||||||
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| Title | LPHT-ring in Vibrio cholerae at disassembled, closed state | ||||||||||||||||||||||||||||||
Components |
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Keywords | MOTOR PROTEIN / In situ cryo-EM / sheathed flagellar motor / Vibrio cholerae / T-ring / MotX / C26 assembled state | ||||||||||||||||||||||||||||||
| Function / homology | Function and homology informationbacterial-type flagellum basal body, distal rod, L ring / bacterial-type flagellum basal body, distal rod, P ring / cytoskeletal motor activity / bacterial-type flagellum-dependent cell motility / cell outer membrane / outer membrane-bounded periplasmic space / structural molecule activity Similarity search - Function | ||||||||||||||||||||||||||||||
| Biological species | Vibrio cholerae O1 biovar El Tor str. N16961 (bacteria) | ||||||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.57 Å | ||||||||||||||||||||||||||||||
Authors | Guo, W. / Yue, J. | ||||||||||||||||||||||||||||||
| Funding support | United States, 2items
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Citation | Journal: To Be PublishedTitle: In-situ cryo-EM structures reveal mechanisms of sheathed flagellar assembly, rotation, and disassembly in Vibrio cholerae Authors: Wangbiao, G. / Jian, Y. / Jin, H.P. / Fitnat, Y. / Jun, L. | ||||||||||||||||||||||||||||||
| History |
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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 | 9yec.cif.gz | 6.9 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9yec.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9yec.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ye/9yec ftp://data.pdbj.org/pub/pdb/validation_reports/ye/9yec | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 72847MC ![]() 9ydoC ![]() 9ydsC ![]() 9ydtC ![]() 9ydxC ![]() 9yedC ![]() 9yeeC ![]() 9yfgC ![]() 9yh6C 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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| 1 |
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Components
-Protein , 4 types, 130 molecules AaAbAcAdAeAfAgAhAiAjAkAlAmAnAoApAqArAsAtAuAvAwAxAyAzBaBbBcBd...
| #1: Protein | Mass: 27541.480 Da / Num. of mol.: 26 / Source method: isolated from a natural source Source: (natural) Vibrio cholerae O1 biovar El Tor str. N16961 (bacteria)References: UniProt: Q9KQ13 #2: Protein | Mass: 37694.059 Da / Num. of mol.: 26 / Source method: isolated from a natural source Source: (natural) Vibrio cholerae O1 biovar El Tor str. N16961 (bacteria)References: UniProt: Q9KQ14 #3: Protein | Mass: 42647.734 Da / Num. of mol.: 26 / Source method: isolated from a natural source Source: (natural) Vibrio cholerae O1 biovar El Tor str. N16961 (bacteria)References: UniProt: Q9KPZ9 #6: Protein | Mass: 16459.971 Da / Num. of mol.: 52 / Source method: isolated from a natural source Source: (natural) Vibrio cholerae O1 biovar El Tor str. N16961 (bacteria)References: UniProt: Q9KQ01 |
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-Sodium-type flagellar protein ... , 2 types, 52 molecules DaDbDcDdDeDfDgDhDiDjDkDlDmDnDoDpDqDrDsDtDuDvDwDxDyDzEaEbEcEd...
| #4: Protein | Mass: 33587.746 Da / Num. of mol.: 26 / Source method: isolated from a natural source Source: (natural) Vibrio cholerae O1 biovar El Tor str. N16961 (bacteria)References: UniProt: Q9KT95 #5: Protein | Mass: 24278.615 Da / Num. of mol.: 26 / Source method: isolated from a natural source Source: (natural) Vibrio cholerae O1 biovar El Tor str. N16961 (bacteria)References: UniProt: Q9KNX9 |
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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: CELL / 3D reconstruction method: single particle reconstruction |
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Sample preparation
| Component | Name: Vibrio cholerae DflhG / Type: CELL / Entity ID: all / Source: NATURAL |
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| Source (natural) | Organism: Vibrio cholerae O1 biovar El Tor str. N16961 (bacteria) |
| Buffer solution | pH: 7.4 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Vitrification | Cryogen name: ETHANE-PROPANE |
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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: OTHER |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2200 nm / Nominal defocus min: 1600 nm / Cs: 2.7 mm / C2 aperture diameter: 100 µm |
| Image recording | Electron dose: 70 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 | ||||||||||||||||||||||||
| Symmetry | Point symmetry: C13 (13 fold cyclic) | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3.57 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 25553 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refinement | Cross valid method: NONE Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2 | ||||||||||||||||||||||||
| Displacement parameters | Biso mean: 136.35 Å2 | ||||||||||||||||||||||||
| Refine LS restraints |
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Movie
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About Yorodumi




Vibrio cholerae O1 biovar El Tor str. N16961 (bacteria)
United States, 2items
Citation
















PDBj






FIELD EMISSION GUN