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Yorodumi- PDB-9ygm: Babesia divergens ribosome structure by single-particle cryo-EM (... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 9ygm | ||||||||||||||||||
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| Title | Babesia divergens ribosome structure by single-particle cryo-EM (3D class3, E-site tRNA) | ||||||||||||||||||
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Keywords | RIBOSOME / tRNAs / RNA modification / 80S | ||||||||||||||||||
| Function / homology | Function and homology informationpreribosome / 90S preribosome / protein-RNA complex assembly / translation regulator activity / ribosomal large subunit biogenesis / maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / maturation of SSU-rRNA / small-subunit processome / chloroplast ...preribosome / 90S preribosome / protein-RNA complex assembly / translation regulator activity / ribosomal large subunit biogenesis / maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / maturation of SSU-rRNA / small-subunit processome / chloroplast / kinase activity / rRNA processing / large ribosomal subunit / ribosomal small subunit assembly / ribosome binding / ribosomal small subunit biogenesis / ribosome biogenesis / 5S rRNA binding / ribosomal large subunit assembly / small ribosomal subunit / cytosolic small ribosomal subunit / small ribosomal subunit rRNA binding / large ribosomal subunit rRNA binding / cytosolic large ribosomal subunit / cytoplasmic translation / negative regulation of translation / rRNA binding / ribosome / translation / structural constituent of ribosome / ribonucleoprotein complex / mRNA binding / nucleolus / RNA binding / zinc ion binding / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||||||||||||||
| Biological species | Babesia divergens (eukaryote) | ||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.7 Å | ||||||||||||||||||
Authors | Gutierrez-Vargas, C. / Izhaki-Tavor, L.S. / Leger-Abraham, M. | ||||||||||||||||||
| Funding support | United States, 2items
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Citation | Journal: bioRxiv / Year: 2025Title: Ribosomal Architecture and rRNA Modification Landscape in the Tick-Borne Parasite . Authors: Cristina Gutierrez-Vargas / Lee S Izhaki-Tavor / Diana Calvopina-Chavez / Caroline D Keroack / Pablo Copello / Manoj T Duraisingh / Mélissa Léger-Abraham / ![]() Abstract: is a tick-borne intracellular apicomplexan parasite responsible for diseases ranging from mild to fatal, with a broadening geographic distribution. Due to the complex life cycle of species, their ... is a tick-borne intracellular apicomplexan parasite responsible for diseases ranging from mild to fatal, with a broadening geographic distribution. Due to the complex life cycle of species, their survival depends on the precise control of gene expression, which is primarily regulated by epigenetic, transcriptional, and post-transcriptional mechanisms. High-resolution structural information on key components of the translation machinery, such as ribosomes, could aid in the development of antiparasitic drugs. Here, we report cryo-EM ribosome structures (2.6 Å) from the tick-borne apicomplexan pathogen , showing associated tRNAs, an mRNA fragment, and RACK1, a signaling scaffold crucial to translation regulation. Density map analysis displays ribosome regions at atomic resolution (1.7 Å), which, when combined with nanopore sequencing, enabled the comprehensive identification of rRNA modifications, including modifications unreported in other organisms. The new rRNA modifications localize not only to the reduced rRNA expansion segments but also to functionally essential ribosomal sites, uncovering new avenues for therapeutic intervention against babesiosis. | ||||||||||||||||||
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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 | 9ygm.cif.gz | 5.4 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9ygm.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9ygm.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/yg/9ygm ftp://data.pdbj.org/pub/pdb/validation_reports/yg/9ygm | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 72933MC ![]() 9yxbC C: citing same article ( M: map data used to model this data |
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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
-RNA chain , 5 types, 5 molecules L3L4L5S7S1
| #1: RNA chain | Mass: 39408.461 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Babesia divergens (eukaryote) / Strain: Rouen 1987 |
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| #73: RNA chain | Mass: 50963.242 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Babesia divergens (eukaryote) / Strain: Rouen 1987 / References: GenBank: 149798938 |
| #74: RNA chain | Mass: 1073104.375 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Babesia divergens (eukaryote) / Strain: Rouen 1987 |
| #75: RNA chain | Mass: 23774.059 Da / Num. of mol.: 1 / Source method: isolated from a natural source Details: The E-site tRNA (PDB 3J7A) was docked into the ribosome using ChimeraX and further refined in PHENIX. Source: (natural) Babesia divergens (eukaryote) / Strain: Rouen 1987 |
| #76: RNA chain | Mass: 556419.688 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Babesia divergens (eukaryote) / Strain: Rouen 1987 |
+60S ribosomal protein ... , 42 types, 42 molecules LBLCLELFLGLJLKLPLQLULVLZLaLbLdLeLfLgLDLILLLMLNLOLRLSLTLXLcLh...
+40S ribosomal protein ... , 32 types, 32 molecules SASBSDSESFSGSISJSKSPSTSUSYSbScSeSCSHSLSMSQSRSSSWSdSNSZSaSfSVSOSX
-Protein , 1 types, 1 molecules Sg
| #65: Protein | Mass: 35573.270 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: Receptor for Activated C Kinase 1 / Source: (natural) Babesia divergens (eukaryote) / Strain: Rouen 1987 / References: UniProt: A0AAD9GHI1 |
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-Non-polymers , 4 types, 201 molecules 






| #81: Chemical | ChemComp-MG / #82: Chemical | ChemComp-ZN / #83: Chemical | ChemComp-K / #84: Water | ChemComp-HOH / | |
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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: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
| Component | Name: 80S ribosome / Type: RIBOSOME / Entity ID: #1-#63, #80, #64-#79 / Source: NATURAL | ||||||||||||||||||||||||
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| Source (natural) | Organism: Babesia divergens (eukaryote) / Strain: Rouen 1987 | ||||||||||||||||||||||||
| Buffer solution | pH: 7.4 | ||||||||||||||||||||||||
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| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||||||
| Specimen support | Details: The grid had an additional ultrathin continuous carbon layer (2 nm) Grid material: COPPER / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R1.2/1.3 | ||||||||||||||||||||||||
| Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277.15 K |
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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 magnification: 105000 X / Nominal defocus max: 2200 nm / Nominal defocus min: 800 nm / Cs: 2.7 mm / C2 aperture diameter: 50 µm |
| Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
| Image recording | Average exposure time: 1.4 sec. / Electron dose: 42 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) / Num. of real images: 12144 |
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Processing
| EM software |
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Particle selection | Num. of particles selected: 1259788 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| 3D reconstruction | Resolution: 2.7 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 261009 / Num. of class averages: 1 / Symmetry type: POINT | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Atomic model building | Protocol: RIGID BODY FIT Details: Initial docking and fitting was done in UCSF ChimeraX for the ribosomal proteins using AlphaFold2 predicted models, except for eL41; the T. gondii eL41 chain (PDB 5XXB) served as the initial ...Details: Initial docking and fitting was done in UCSF ChimeraX for the ribosomal proteins using AlphaFold2 predicted models, except for eL41; the T. gondii eL41 chain (PDB 5XXB) served as the initial model. The T. gondii PDBs 5XXU and 5XXB were also fit with UCSF ChimeraX and used for initial model building of the Babesia divergens rRNAs. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Atomic model building | 3D fitting-ID: 1
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Babesia divergens (eukaryote)
United States, 2items
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