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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) | |||||||||||||||||||||||||||
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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: Nat Struct Mol Biol / Year: 2025Title: Atomic models of the Toxoplasma cell invasion machinery. Authors: Jianwei Zeng / Yong Fu / Pengge Qian / Wei Huang / Qingwei Niu / Wandy L Beatty / Alan Brown / L David Sibley / Rui Zhang / ![]() Abstract: Apicomplexan parasites, responsible for toxoplasmosis, cryptosporidiosis and malaria, invade host cells through a unique gliding motility mechanism powered by actomyosin motors and a dynamic ...Apicomplexan parasites, responsible for toxoplasmosis, cryptosporidiosis and malaria, invade host cells through a unique gliding motility mechanism powered by actomyosin motors and a dynamic organelle called the conoid. Here, using cryo-electron microscopy, we determined structures of four essential complexes of the Toxoplasma gondii conoid: the preconoidal P2 ring, tubulin-based conoid fibers, and the subpellicular and intraconoidal microtubules. Our analysis identified 40 distinct conoid proteins, several of which are essential for parasite lytic growth, as revealed through genetic disruption studies. Comparative analysis of the tubulin-containing complexes sheds light on their functional specialization by microtubule-associated proteins, while the structure of the preconoidal ring pinpoints the site of actin polymerization and initial translocation, enhancing our mechanistic understanding of gliding motility and, therefore, parasite invasion. | |||||||||||||||||||||||||||
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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 | 8.2 MB | Display | wwPDB validaton report |
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| Full document | 9y9z_full_validation.pdf.gz | 8.3 MB | Display | |
| Data in XML | 9y9z_validation.xml.gz | 1.1 MB | Display | |
| Data in CIF | 9y9z_validation.cif.gz | 1.7 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 ![]() 9ya0C ![]() 9ya1C ![]() 9ya2C ![]() 9ya3C 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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United States, 1items
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FIELD EMISSION GUN