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Yorodumi- PDB-9y9z: Cryo-EM structure of conoid fiber from Toxoplasma gondii (24-nm r... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 9y9z | |||||||||||||||||||||||||||
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| Title | Cryo-EM structure of conoid fiber from Toxoplasma gondii (24-nm repeat) | |||||||||||||||||||||||||||
Components |
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Keywords | STRUCTURAL PROTEIN / Tubulin / Microtubule / Microtubule Inner Protein / Microtubule-associated Protein / Toxoplasma gondii / conoid / conoid fiber | |||||||||||||||||||||||||||
| Function / homology | Function and homology informationcondensin complex / mitotic chromosome condensation / microtubule polymerization / microtubule-based process / condensed chromosome / tubulin binding / structural constituent of cytoskeleton / microtubule binding / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / microtubule ...condensin complex / mitotic chromosome condensation / microtubule polymerization / microtubule-based process / condensed chromosome / tubulin binding / structural constituent of cytoskeleton / microtubule binding / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / microtubule / cytoskeleton / intracellular signal transduction / hydrolase activity / GTPase activity / chromatin binding / chromatin / GTP binding / metal ion binding / cytoplasm Similarity search - Function | |||||||||||||||||||||||||||
| Biological species | ![]() | |||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.14 Å | |||||||||||||||||||||||||||
Authors | Zeng, J. / Zhang, R. | |||||||||||||||||||||||||||
| Funding support | United States, 1items
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Citation | Journal: To Be PublishedTitle: Atomic models of the conoid, the cell invasion machinery of the human parasite Toxoplasma gondii Authors: Zeng, J. / Fu, Y. / Qian, P. / Sibley, L.D. / Zhang, R. | |||||||||||||||||||||||||||
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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 | 9y9z.cif.gz | 19.1 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9y9z.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9y9z.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 9y9z_validation.pdf.gz | 12.1 MB | Display | wwPDB validaton report |
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| Full document | 9y9z_full_validation.pdf.gz | 13.4 MB | Display | |
| Data in XML | 9y9z_validation.xml.gz | 2.3 MB | Display | |
| Data in CIF | 9y9z_validation.cif.gz | 3.6 MB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/y9/9y9z ftp://data.pdbj.org/pub/pdb/validation_reports/y9/9y9z | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 72715MC 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 , 14 types, 378 molecules ABCDEFGHIJKLMNOPQRSTUVWXYZ12ab...
| #1: Protein | Mass: 106251.133 Da / Num. of mol.: 54 / Source method: isolated from a natural source / Source: (natural) ![]() #2: Protein | Mass: 47976.344 Da / Num. of mol.: 14 / Source method: isolated from a natural source / Source: (natural) ![]() #3: Protein | Mass: 50166.645 Da / Num. of mol.: 63 / Source method: isolated from a natural source / Source: (natural) ![]() #4: Protein | Mass: 50119.121 Da / Num. of mol.: 57 / Source method: isolated from a natural source / Source: (natural) ![]() #5: Protein | Mass: 29529.971 Da / Num. of mol.: 41 / Source method: isolated from a natural source / Source: (natural) ![]() #6: Protein | Mass: 114592.602 Da / Num. of mol.: 7 / Source method: isolated from a natural source / Source: (natural) ![]() #7: Protein | Mass: 46600.648 Da / Num. of mol.: 24 / Source method: isolated from a natural source / Source: (natural) ![]() #8: Protein | Mass: 56022.809 Da / Num. of mol.: 9 / Source method: isolated from a natural source / Source: (natural) ![]() #9: Protein | Mass: 62988.641 Da / Num. of mol.: 7 / Source method: isolated from a natural source / Source: (natural) ![]() #10: Protein | Mass: 67410.492 Da / Num. of mol.: 28 / Source method: isolated from a natural source / Source: (natural) ![]() #11: Protein | Mass: 38845.750 Da / Num. of mol.: 5 / Source method: isolated from a natural source / Source: (natural) ![]() #12: Protein | Mass: 80452.414 Da / Num. of mol.: 35 / Source method: isolated from a natural source / Source: (natural) ![]() #13: Protein | Mass: 97829.719 Da / Num. of mol.: 7 / Source method: isolated from a natural source / Source: (natural) ![]() #14: Protein | Mass: 29261.402 Da / Num. of mol.: 27 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Non-polymers , 3 types, 174 molecules 




| #15: Chemical | ChemComp-GTP / #16: Chemical | ChemComp-MG / #17: Chemical | ChemComp-GDP / |
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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: FILAMENT / 3D reconstruction method: single particle reconstruction |
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Sample preparation
| Component | Name: conoid fiber from Toxoplasma gondii (24-nm repeat) / Type: COMPLEX / Entity ID: #1-#14 / Source: NATURAL |
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| Molecular weight | Experimental value: NO |
| Source (natural) | 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: TFS KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 25000 nm / Nominal defocus min: 5000 nm |
| Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (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: 3.14 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 95409 / Symmetry type: POINT |
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About Yorodumi





United States, 1items
Citation
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FIELD EMISSION GUN