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Yorodumi- PDB-9i05: Cryo-EM structure of the large subunit of the mitochondrial ribos... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 9i05 | |||||||||||||||||||||||||||
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| Title | Cryo-EM structure of the large subunit of the mitochondrial ribosome from Toxoplasma gondii | |||||||||||||||||||||||||||
Components |
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Keywords | RIBOSOME / Toxoplasma gondii / parasite / mitochondrial ribosome / LSU / large subunit | |||||||||||||||||||||||||||
| Function / homology | Function and homology informationregulation of mitochondrial mRNA stability / ribonucleoprotein granule / mitochondrial RNA processing / mitochondrial large ribosomal subunit / mitochondrial translation / cyclosporin A binding / peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / ubiquitin-protein transferase activity / protein folding ...regulation of mitochondrial mRNA stability / ribonucleoprotein granule / mitochondrial RNA processing / mitochondrial large ribosomal subunit / mitochondrial translation / cyclosporin A binding / peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / ubiquitin-protein transferase activity / protein folding / large ribosomal subunit / transferase activity / 5S rRNA binding / large ribosomal subunit rRNA binding / cytosolic large ribosomal subunit / negative regulation of translation / rRNA binding / structural constituent of ribosome / ribosome / translation / mitochondrial matrix / DNA-binding transcription factor activity / ribonucleoprotein complex / mRNA binding / DNA binding / RNA binding / nucleus / membrane / cytoplasm Similarity search - Function | |||||||||||||||||||||||||||
| Biological species | ![]() | |||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.2 Å | |||||||||||||||||||||||||||
Authors | Tobiasson, V. / Shikha, S. / Muhleip, A. | |||||||||||||||||||||||||||
| Funding support | United Kingdom, 1items
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Citation | Journal: Nat Commun / Year: 2025Title: Numerous rRNA molecules form the apicomplexan mitoribosome via repurposed protein and RNA elements. Authors: Shikha Shikha / Victor Tobiasson / Mariana Ferreira Silva / Jana Ovciarikova / Dario Beraldi / Alexander Mühleip / Lilach Sheiner / ![]() Abstract: Mitochondrial ribosomes (mitoribosomes) are essential, and their function of synthesising mitochondrial proteins is universal. The core of almost all mitoribosomes is formed from a small number of ...Mitochondrial ribosomes (mitoribosomes) are essential, and their function of synthesising mitochondrial proteins is universal. The core of almost all mitoribosomes is formed from a small number of long and self-folding rRNA molecules. In contrast, the mitoribosome of the apicomplexan parasite Toxoplasma gondii assembles from over 50 extremely short rRNA molecules. Here, we use cryo-EM to discover the features that enable this unusual mitoribosome to perform its function. We reveal that poly-A tails added to rRNA molecules are integrated into the ribosome, and we demonstrate their essentiality for mitoribosome formation and for parasite survival. This is a distinct function for poly-A tails, which are otherwise known primarily as stabilisers of messenger RNAs. Furthermore, while ribosomes typically consist of unique rRNA sequences, here nine sequences are used twice, each copy integrated in a different mitoribosome domain, revealing one of the mechanisms enabling the extreme mitochondrial genome reduction characteristic to Apicomplexa and to a large group of related microbial eukaryotes. Finally, several transcription factor-like proteins are repurposed to compensate for reduced or lost critical ribosomal domains, including members of the ApiAP2 family thus far considered to be DNA-binding transcription factors. | |||||||||||||||||||||||||||
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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 | 9i05.cif.gz | 7.7 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9i05.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9i05.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 9i05_validation.pdf.gz | 1.4 MB | Display | wwPDB validaton report |
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| Full document | 9i05_full_validation.pdf.gz | 1.4 MB | Display | |
| Data in XML | 9i05_validation.xml.gz | 225.4 KB | Display | |
| Data in CIF | 9i05_validation.cif.gz | 340.6 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/i0/9i05 ftp://data.pdbj.org/pub/pdb/validation_reports/i0/9i05 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 52551MC ![]() 9hqvC 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
+Putative LSU ribosomal protein ... , 2 types, 2 molecules AaAh
+Large ribosomal subunit protein ... , 10 types, 10 molecules AbAcAnApAqAuABADAFXe
+Protein , 34 types, 34 molecules AdAlAoAsAvAxAyAzAAAEAGAHXaXbXcXfXgXkXmXoXpXqXsXtXxXyXAXBXCXD...
+Ribosomal protein ... , 4 types, 4 molecules AeAiACXH
+Putative ribosomal protein ... , 3 types, 3 molecules AfAmAt
+Putative 50S ribosomal protein ... , 4 types, 4 molecules AgAjAkAw
+Ribosomal l25 family ... , 2 types, 2 molecules ArUa
+RAP domain-containing ... , 7 types, 8 molecules AIXdXhXiXjXlXvXr
+AP2 domain transcription factor ... , 2 types, 2 molecules XnXz
+Transmembrane ... , 2 types, 2 molecules XwXI
+Protein/peptide , 5 types, 5 molecules UbUcUdUeUf
+RNA chain , 32 types, 32 molecules RARBRCRDRERFRGRIRJRKRLRMRNRORPRQRSRTRURVRWRXRYRZRaRbRcRdRfRgRhRi
+Non-polymers , 2 types, 3 molecules 


+Details
-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: mitochondrial ribososome from Toxoplasma gondii / Type: RIBOSOME / Entity ID: #1-#106 / Source: NATURAL |
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| Molecular weight | Experimental value: NO |
| Source (natural) | Organism: ![]() |
| Buffer solution | pH: 7.4 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Specimen support | Grid type: Quantifoil R2/1 |
| Vitrification | Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277 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 defocus max: 1600 nm / Nominal defocus min: 600 nm |
| Image recording | Electron dose: 35 e/Å2 / Film or detector model: GATAN K3 BIOCONTINUUM (6k x 4k) |
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Processing
| EM software | Name: PHENIX / Version: 1.21rc1_5058: / Category: model refinement | ||||||||||||||||||||||||
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 2.2 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 375745 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refine LS restraints |
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About Yorodumi





United Kingdom, 1items
Citation




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FIELD EMISSION GUN