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Open data
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Basic information
| Entry | Database: PDB / ID: 9uwh | |||||||||
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| Title | human mitoribosome trapped by retapamulin | |||||||||
Components |
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Keywords | RIBOSOME / mitoribosome / retapamulin | |||||||||
| Function / homology | Function and homology informationrRNA import into mitochondrion / mitochondrial translational termination / mitochondrial transcription / mitochondrial translational elongation / mitochondrial ribosome assembly / Mitochondrial translation elongation / Mitochondrial translation termination / translation release factor activity, codon nonspecific / Mitochondrial translation initiation / translation release factor activity ...rRNA import into mitochondrion / mitochondrial translational termination / mitochondrial transcription / mitochondrial translational elongation / mitochondrial ribosome assembly / Mitochondrial translation elongation / Mitochondrial translation termination / translation release factor activity, codon nonspecific / Mitochondrial translation initiation / translation release factor activity / negative regulation of mitotic nuclear division / mitochondrial large ribosomal subunit / peptidyl-tRNA hydrolase / mitochondrial ribosome / mitochondrial small ribosomal subunit / Hydrolases; Acting on ester bonds; Endoribonucleases producing 5'-phosphomonoesters / peptidyl-tRNA hydrolase activity / mitochondrial translation / apoptotic mitochondrial changes / positive regulation of proteolysis / ribosomal small subunit binding / anatomical structure morphogenesis / RNA processing / Mitochondrial protein degradation / rescue of stalled cytosolic ribosome / cellular response to leukemia inhibitory factor / apoptotic signaling pathway / fibrillar center / cell junction / double-stranded RNA binding / regulation of translation / ribosomal small subunit assembly / 5S rRNA binding / small ribosomal subunit / small ribosomal subunit rRNA binding / large ribosomal subunit rRNA binding / endonuclease activity / nuclear membrane / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / tRNA binding / cell population proliferation / negative regulation of translation / mitochondrial inner membrane / rRNA binding / nuclear body / structural constituent of ribosome / ribosome / translation / mitochondrial matrix / ribonucleoprotein complex / protein domain specific binding / nucleotide binding / intracellular membrane-bounded organelle / mRNA binding / apoptotic process / positive regulation of DNA-templated transcription / GTP binding / nucleolus / mitochondrion / extracellular space / RNA binding / nucleoplasm / nucleus / plasma membrane / cytosol / cytoplasm Similarity search - Function | |||||||||
| Biological species | Homo sapiens (human) | |||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3 Å | |||||||||
Authors | Ando, Y. / Nureki, O. / Itoh, Y. | |||||||||
| Funding support | Japan, 2items
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Citation | Journal: Mol Cell / Year: 2025Title: Monitoring the complexity and dynamics of mitochondrial translation. Authors: Taisei Wakigawa / Mari Mito / Yushin Ando / Haruna Yamashiro / Kotaro Tomuro / Haruna Tani / Kazuhito Tomizawa / Takeshi Chujo / Asuteka Nagao / Takeo Suzuki / Osamu Nureki / Fan-Yan Wei / ...Authors: Taisei Wakigawa / Mari Mito / Yushin Ando / Haruna Yamashiro / Kotaro Tomuro / Haruna Tani / Kazuhito Tomizawa / Takeshi Chujo / Asuteka Nagao / Takeo Suzuki / Osamu Nureki / Fan-Yan Wei / Yuichi Shichino / Yuzuru Itoh / Tsutomu Suzuki / Shintaro Iwasaki / ![]() Abstract: Since mitochondrial translation leads to the synthesis of the essential oxidative phosphorylation (OXPHOS) subunits, exhaustive and quantitative delineation of mitoribosome traversal is needed. Here, ...Since mitochondrial translation leads to the synthesis of the essential oxidative phosphorylation (OXPHOS) subunits, exhaustive and quantitative delineation of mitoribosome traversal is needed. Here, we developed a variety of high-resolution mitochondrial ribosome profiling derivatives and revealed the intricate regulation of mammalian mitochondrial translation. Harnessing a translation inhibitor, retapamulin, our approach assessed the stoichiometry and kinetics of mitochondrial translation flux, such as the number of mitoribosomes on a transcript, the elongation rate, and the initiation rate. We also surveyed the impacts of modifications at the anticodon stem loop in mitochondrial tRNAs (mt-tRNAs), including all possible modifications at the 34th position, in cells deleting the corresponding enzymes and derived from patients, as well as in mouse tissues. Moreover, a retapamulin-assisted derivative and mito-disome profiling revealed mitochondrial translation initiation factor (mtIF) 3-mediated translation initiation from internal open reading frames (ORFs) and programmed mitoribosome collision sites across the mitochondrial transcriptome. Our work provides a useful platform for investigating protein synthesis within the energy powerhouse of the cell. | |||||||||
| History |
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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 | 9uwh.cif.gz | 4.3 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9uwh.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9uwh.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/uw/9uwh ftp://data.pdbj.org/pub/pdb/validation_reports/uw/9uwh | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 64554MC 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
-RNA chain , 5 types, 5 molecules ABAAAxAz
| #1: RNA chain | Mass: 500727.125 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: GenBank: 2756414513 |
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| #2: RNA chain | Mass: 22989.752 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: GenBank: 1896813692 |
| #25: RNA chain | Mass: 306218.312 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: GenBank: 1858621102 |
| #56: RNA chain | Mass: 22692.508 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) |
| #57: RNA chain | Mass: 2489.489 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) |
+Large ribosomal subunit protein ... , 51 types, 51 molecules DEFHIJKLMNOPQRSTUVWXYZ01234567...
+Small ribosomal subunit protein ... , 29 types, 29 molecules ABACADAEAFAGAHAIAJAKALAMANAOAPARASATAUAVAWAXAYAZA0A1A2A3A4
-Protein , 1 types, 1 molecules AQ
| #41: Protein | Mass: 10659.494 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: A0A2J8VEN6 |
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-Non-polymers , 10 types, 273 molecules 


















| #87: Chemical | ChemComp-MG / #88: Chemical | ChemComp-K / #89: Chemical | ChemComp-G34 / | #90: Chemical | ChemComp-VAL / | #91: Chemical | ChemComp-NAD / | #92: Chemical | ChemComp-SPD / | #93: Chemical | #94: Chemical | #95: Chemical | ChemComp-ATP / | #96: 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: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
| Component | Name: human mitoribosome trapped by retapamulin / Type: RIBOSOME / Entity ID: #1-#8, #10-#18, #20-#40, #42-#52, #54-#86 / Source: NATURAL |
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| Molecular weight | Experimental value: NO |
| Source (natural) | Organism: Homo sapiens (human) |
| Buffer solution | pH: 7.5 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Specimen support | Grid material: GOLD / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R2/1 |
| Vitrification | Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 297 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: 800 nm |
| Image recording | Electron dose: 30 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
| EM software | Name: PHENIX / Version: 1.20.1_4487: / Category: model refinement | ||||||||||||||||||||||||
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 114776 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refine LS restraints |
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About Yorodumi




Homo sapiens (human)
Japan, 2items
Citation


PDBj











































FIELD EMISSION GUN