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Yorodumi- PDB-9pr4: In Situ Structure of the Human Mitochondrial Large Subunit 39S in... -
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Basic information
| Entry | Database: PDB / ID: 9pr4 | ||||||||||||||||||||||||||||||
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| Title | In Situ Structure of the Human Mitochondrial Large Subunit 39S in Complex with TACO1 | ||||||||||||||||||||||||||||||
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Keywords | RIBOSOME / mitochondria / mitoribosome / inner membrane | ||||||||||||||||||||||||||||||
| Function / homology | Function and homology informationComplex IV assembly / motor learning / mitochondrial protein quality control / protein insertion into mitochondrial inner membrane from matrix / negative regulation of oxidoreductase activity / mitochondrial ribosome binding / membrane insertase activity / regulation of mitochondrial translation / mitochondrial respiratory chain complex IV assembly / Complex I biogenesis ...Complex IV assembly / motor learning / mitochondrial protein quality control / protein insertion into mitochondrial inner membrane from matrix / negative regulation of oxidoreductase activity / mitochondrial ribosome binding / membrane insertase activity / regulation of mitochondrial translation / mitochondrial respiratory chain complex IV assembly / Complex I biogenesis / rRNA import into mitochondrion / mitochondrial transcription / mitochondrial translational termination / negative regulation of ATP-dependent activity / Mitochondrial ribosome-associated quality control / mitochondrial translational elongation / Mitochondrial translation elongation / translation release factor activity, codon nonspecific / Mitochondrial translation initiation / mitochondrial proton-transporting ATP synthase complex assembly / Mitochondrial translation termination / translation release factor activity / mitochondrial large ribosomal subunit / peptidyl-tRNA hydrolase / mitochondrial ribosome / Hydrolases; Acting on ester bonds; Endoribonucleases producing 5'-phosphomonoesters / mitochondrial small ribosomal subunit / peptidyl-tRNA hydrolase activity / mitochondrial translation / mitochondrial respiratory chain complex I assembly / anatomical structure morphogenesis / RNA processing / Mitochondrial protein degradation / rescue of stalled cytosolic ribosome / aerobic respiration / cellular response to leukemia inhibitory factor / protein tetramerization / mitochondrial membrane / fibrillar center / cell junction / double-stranded RNA binding / 5S rRNA binding / small ribosomal subunit rRNA binding / large ribosomal subunit rRNA binding / endonuclease activity / mitochondrial inner membrane / negative regulation of translation / rRNA binding / nuclear body / structural constituent of ribosome / ribosome / translation / mitochondrial matrix / ribonucleoprotein complex / protein domain specific binding / nucleotide binding / mRNA binding / apoptotic process / positive regulation of DNA-templated transcription / nucleolus / protein homodimerization activity / protein-containing complex / mitochondrion / extracellular space / RNA binding / nucleoplasm / nucleus / plasma membrane / cytosol Similarity search - Function | ||||||||||||||||||||||||||||||
| Biological species | Homo sapiens (human) | ||||||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.77 Å | ||||||||||||||||||||||||||||||
Authors | Wang, S. / Xiong, Y. / Zhang, Y. | ||||||||||||||||||||||||||||||
| Funding support | United States, 1items
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Citation | Journal: Nat Commun / Year: 2026Title: Structural basis of TACO1-mediated efficient mitochondrial translation. Authors: Shuhui Wang / Michele Brischigliaro / Yuekang Zhang / Chunxiang Wu / Wei Zheng / Antoni Barrientos / Yong Xiong / ![]() Abstract: Translation elongation is a universally conserved step in protein synthesis, relying on elongation factors that engage the ribosomal L7/L12 stalk to mediate aminoacyl-tRNA delivery, accommodation, ...Translation elongation is a universally conserved step in protein synthesis, relying on elongation factors that engage the ribosomal L7/L12 stalk to mediate aminoacyl-tRNA delivery, accommodation, and ribosomal translocation. Using in organello cryo-electron microscopy, we reveal how the mitochondrial translation accelerator TACO1 promotes efficient elongation on human mitoribosomes. TACO1 binds the mitoribosomal region typically bound by elongation factor Tu (mtEF-Tu), bridging the large and small subunits via contacts with 16S rRNA, bL12m, A-site tRNA, and uS12m. While active throughout elongation, TACO1 is especially critical when translating polyproline motifs. Its absence prolongs mtEF-Tu residence in A/T states, causes persistent mitoribosomal stalling and premature subunit dissociation. Structural analyses indicate that TACO1 competes with mtEF-Tu for mitoribosome binding, stabilizes A-site tRNA, and enhances peptidyl transfer through a mechanism distinct from EF-P and eIF5A. These findings suggest that bacterial TACO1 orthologs may serve analogous roles, highlighting an evolutionarily conserved strategy for maintaining elongation efficiency during challenging translation events. | ||||||||||||||||||||||||||||||
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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 | 9pr4.cif.gz | 2.8 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9pr4.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9pr4.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/pr/9pr4 ftp://data.pdbj.org/pub/pdb/validation_reports/pr/9pr4 | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 71797MC ![]() 9olfC ![]() 9praC ![]() 9prdC ![]() 9prqC ![]() 9prxC ![]() 9ps0C ![]() 9ps7C ![]() 9psiC ![]() 9psmC 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
+39S ribosomal protein ... , 46 types, 52 molecules 0123456789DEFGtuvwxyHIJLMNOPQR...
-Protein , 5 types, 5 molecules CoqpOX
| #11: Protein | Mass: 32532.180 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9BSH4 |
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| #46: Protein | Mass: 12292.333 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9BQC6 |
| #47: Protein | Mass: 25426.895 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q8TAE8 |
| #53: Protein | Mass: 23674.203 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q14197, peptidyl-tRNA hydrolase |
| #55: Protein | Mass: 48574.633 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q15070 |
-Large ribosomal subunit protein ... , 3 types, 3 molecules Kkz
| #19: Protein | Mass: 20617.828 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: H2QWN0 |
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| #42: Protein | Mass: 12020.701 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q96EL3 |
| #49: Protein | Mass: 36967.746 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9BYD6 |
-Protein/peptide , 1 types, 1 molecules n
| #45: Protein/peptide | Mass: 3677.524 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) |
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-RNA chain , 2 types, 2 molecules AB
| #50: RNA chain | Mass: 499786.438 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: GenBank: 2756414513 |
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| #57: 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 |
-Non-polymers , 7 types, 184 molecules 












| #58: Chemical | | #59: Chemical | ChemComp-K / #60: Chemical | ChemComp-MG / #61: Chemical | ChemComp-FES / | #62: Chemical | #63: Chemical | ChemComp-PUT / | #64: Chemical | ChemComp-VAL / | |
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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: mitochondria / Type: RIBOSOME Entity ID: #1-#10, #50, #11-#14, #16, #18-#29, #31-#34, #49, #15, #17, #30, #35-#41, #43-#48, #51-#56, #42, #57 Source: NATURAL |
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| Molecular weight | Experimental value: NO |
| Source (natural) | Organism: Homo sapiens (human) |
| Buffer solution | pH: 7.4 |
| 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: 4000 nm / Nominal defocus min: 1000 nm |
| Image recording | Electron dose: 55 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 2.77 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 131357 / Symmetry type: POINT | ||||||||||||||||||||||||
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Homo sapiens (human)
United States, 1items
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