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Open data
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Basic information
| Entry | Database: PDB / ID: 9olf | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Title | Membrane-associated human mitoribosome in complex with TACO1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Keywords | RIBOSOME / mitochondria / mitoribosome / inner membrane | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Function / homology | Function and homology informationnegative regulation of mitochondrial RNA catabolic process / Complex IV assembly / motor learning / mitochondrial protein quality control / Mitochondrial RNA degradation / protein insertion into mitochondrial inner membrane from matrix / negative regulation of oxidoreductase activity / mitochondrial ribosome binding / membrane insertase activity / mitochondrial RNA catabolic process ...negative regulation of mitochondrial RNA catabolic process / Complex IV assembly / motor learning / mitochondrial protein quality control / Mitochondrial RNA degradation / protein insertion into mitochondrial inner membrane from matrix / negative regulation of oxidoreductase activity / mitochondrial ribosome binding / membrane insertase activity / mitochondrial RNA catabolic process / 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 / flagellated sperm motility / mitochondrial ribosome assembly / Mitochondrial translation elongation / translation release factor activity, codon nonspecific / Mitochondrial translation initiation / mitochondrial proton-transporting ATP synthase complex assembly / Mitochondrial translation termination / negative regulation of mitotic nuclear division / 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 / nuclear inner membrane / peptidyl-tRNA hydrolase activity / mitochondrial translation / mitochondrion transport along microtubule / apoptotic mitochondrial changes / nuclear outer membrane / mitochondrial nucleoid / mitochondrial respiratory chain complex I assembly / positive regulation of proteolysis / ribosomal small subunit binding / spermatid development / anatomical structure morphogenesis / mRNA transport / single fertilization / sperm flagellum / RNA processing / beta-tubulin binding / Mitochondrial protein degradation / acrosomal vesicle / rescue of stalled cytosolic ribosome / aerobic respiration / condensed nuclear chromosome / cellular response to leukemia inhibitory factor / mitochondrion organization / mRNA 3'-UTR binding / protein tetramerization / apoptotic signaling pathway / autophagy / mitochondrial membrane / fibrillar center / cell junction / single-stranded DNA binding / 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 / microtubule binding / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / microtubule / cytoskeleton / tRNA binding / cell population proliferation / mitochondrial inner membrane / negative regulation of translation / rRNA binding / nuclear body / structural constituent of ribosome / ribosome / translation / mitochondrial matrix / ribonucleoprotein complex / intracellular membrane-bounded organelle / protein domain specific binding / nucleotide binding / mRNA binding / apoptotic process / ubiquitin protein ligase binding / positive regulation of DNA-templated transcription / GTP binding / nucleolus / perinuclear region of cytoplasm / protein homodimerization activity Similarity search - Function | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Biological species | Homo sapiens (human) | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.46 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 | 9olf.cif.gz | 4.8 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9olf.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9olf.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ol/9olf ftp://data.pdbj.org/pub/pdb/validation_reports/ol/9olf | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 70592MC ![]() 9pr4C ![]() 9praC ![]() 9prdC ![]() 9prqC ![]() 9prxC ![]() 9ps0C ![]() 9ps7C ![]() 9psiC ![]() 9psmC ![]() 70619 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...
-RNA chain , 7 types, 7 molecules AAAAwAxAyAzB
| #11: 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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| #19: 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 |
| #45: RNA chain | Mass: 24261.480 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) |
| #46: RNA chain | Mass: 22664.498 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: GenBank: 1896813686 |
| #47: RNA chain | Mass: 24344.541 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) |
| #48: RNA chain | Mass: 10826.415 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) |
| #49: 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 |
-Small ribosomal subunit protein ... , 3 types, 3 molecules A0A2AQ
| #12: Protein | Mass: 25564.354 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P82930 |
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| #14: Protein | Mass: 13393.661 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q96BP2 |
| #35: Protein | Mass: 10659.494 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P82921 |
+28S ribosomal protein ... , 25 types, 25 molecules A1ABACADAEAFAGAHAIAJAKALAMANAOAPARASATAUAVAWAXAYAZ
-Protein , 9 types, 9 molecules A3A4A5A6COXopq
| #15: Protein | Mass: 22395.326 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9NWT8 |
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| #16: Protein | Mass: 78648.547 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q96EY7 |
| #17: Protein | Mass: 158098.359 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P42704 |
| #18: Protein | Mass: 12371.032 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9GZT3 |
| #50: Protein | Mass: 32532.180 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9BSH4 |
| #63: Protein | Mass: 48574.633 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q15070 |
| #89: Protein | Mass: 12292.333 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9BQC6 |
| #90: 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 |
| #91: Protein | Mass: 25426.895 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q8TAE8 |
-Large ribosomal subunit protein ... , 3 types, 3 molecules Kkz
| #58: 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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| #85: Protein | Mass: 12020.701 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q96EL3 |
| #94: 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
| #88: 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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-Non-polymers , 11 types, 279 molecules 




















| #95: Chemical | | #96: Chemical | ChemComp-SPD / #97: Chemical | ChemComp-MG / #98: Chemical | ChemComp-PUT / | #99: Chemical | ChemComp-K / #100: Chemical | #101: Chemical | ChemComp-NAD / | #102: Chemical | #103: Chemical | ChemComp-GDP / | #104: Chemical | ChemComp-ATP / | #105: 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: ORGANELLE OR CELLULAR COMPONENT Entity ID: #1-#11, #50-#53, #55, #57-#62, #64-#69, #71-#74, #94, #54, #56, #70, #76, #78-#79, #81-#89, #91-#92, #77, #80, #90, #93, #20-#26, #28-#42, #44, #12-#15, #48, #43, #17-#19, #27, #63, #75, #46-#47, #45, #16, #49 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: 2.46 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 526704 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refine LS restraints |
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About Yorodumi




Homo sapiens (human)
United States, 1items
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FIELD EMISSION GUN