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Yorodumi- PDB-9hqv: Cryo-EM structure of the small subunit of the mitochondrial ribos... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 9hqv | |||||||||||||||||||||||||||
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| Title | Cryo-EM structure of the small subunit of the mitochondrial ribosome from Toxoplasma gondii | |||||||||||||||||||||||||||
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Keywords | RIBOSOME / Toxoplasma gondii / parasite / mitochondrial ribosome / SSU / large subunit | |||||||||||||||||||||||||||
| Function / homology | Function and homology informationhydro-lyase activity / mitochondrial small ribosomal subunit / mitochondrial translation / isomerase activity / fatty acid metabolic process / small ribosomal subunit / small ribosomal subunit rRNA binding / structural constituent of ribosome / ribosome / translation ...hydro-lyase activity / mitochondrial small ribosomal subunit / mitochondrial translation / isomerase activity / fatty acid metabolic process / small ribosomal subunit / small ribosomal subunit rRNA binding / structural constituent of ribosome / ribosome / translation / ribonucleoprotein complex / mitochondrion / RNA binding / membrane / cytoplasm Similarity search - Function | |||||||||||||||||||||||||||
| Biological species | ![]() | |||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.52 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 | 9hqv.cif.gz | 5.8 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9hqv.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9hqv.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hq/9hqv ftp://data.pdbj.org/pub/pdb/validation_reports/hq/9hqv | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 52348MC ![]() 9i05C 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 , 35 types, 35 molecules BABCBDBcBfBiBpBsBtBvByBzUdUhUjYaYbYcYdYeYfYgYhYiYjYlYnYoYpYr...
+Protein/peptide , 11 types, 12 molecules BBUaUbUcUiUkUlUmUnUoUpUq
+Ribosomal protein, ... , 2 types, 2 molecules BaBo
+Putative 30S ribosomal protein ... , 4 types, 4 molecules BbBhBkBl
+Putative ribosomal protein ... , 6 types, 6 molecules BdBeBgBjBmBn
+Mitochondrial ... , 2 types, 2 molecules BqBx
+Small ribosomal subunit protein ... , 2 types, 2 molecules BrBu
+RAP domain-containing ... , 2 types, 2 molecules YkYm
+RNA chain , 23 types, 23 molecules SASBSCSDSESFSGSHSISJSKSLSMSNSOSPSQSRSSSTSUTPUC
+Non-polymers , 3 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 small ribosomal subunit from Toxoplasma gondii Type: RIBOSOME / Entity ID: #1-#87 / 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 R2/2 |
| Vitrification | Instrument: FEI VITROBOT MARK III / 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 / C2 aperture diameter: 50 µm |
| Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Temperature (min): 70 K |
| Image recording | Electron dose: 36 e/Å2 / Film or detector model: GATAN K2 QUANTUM (4k x 4k) |
| EM imaging optics | Energyfilter name: GIF Quantum LS / Energyfilter slit width: 20 eV |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 2.52 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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