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Open data
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Basic information
| Entry | Database: PDB / ID: 9ojm | ||||||||||||||||||||||||
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| Title | Human mitochondrial 28S PIC with tRNA and mtIF2 | ||||||||||||||||||||||||
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Keywords | RIBOSOME / Mitochondrial Ribosome 28S pre-initiation complex | ||||||||||||||||||||||||
| Function / homology | Function and homology informationmitochondrial translational initiation / translation factor activity, RNA binding / formation of translation preinitiation complex / mitochondrial ribosome assembly / Mitochondrial translation elongation / Mitochondrial translation initiation / Mitochondrial ribosome-associated quality control / Mitochondrial translation termination / mitochondrial ribosome / ribosome disassembly ...mitochondrial translational initiation / translation factor activity, RNA binding / formation of translation preinitiation complex / mitochondrial ribosome assembly / Mitochondrial translation elongation / Mitochondrial translation initiation / Mitochondrial ribosome-associated quality control / Mitochondrial translation termination / mitochondrial ribosome / ribosome disassembly / mitochondrial small ribosomal subunit / mitochondrial translation / apoptotic mitochondrial changes / positive regulation of proteolysis / ribosomal small subunit binding / sperm head-tail coupling apparatus / translation initiation factor activity / Mitochondrial protein degradation / apoptotic signaling pathway / fibrillar center / regulation of translation / small ribosomal subunit / small ribosomal subunit rRNA binding / nuclear membrane / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / tRNA binding / cell population proliferation / mitochondrial inner membrane / rRNA binding / structural constituent of ribosome / ribosome / translation / mitochondrial matrix / mRNA binding / GTPase activity / GTP binding / nucleolus / mitochondrion / RNA binding / nucleoplasm / nucleus / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||||||||||||||||||||
| Biological species | Homo sapiens (human) | ||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.5 Å | ||||||||||||||||||||||||
Authors | Kober, D.L. / Wang, J. | ||||||||||||||||||||||||
| Funding support | United States, 4items
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Citation | Journal: Nat Commun / Year: 2026Title: Mechanisms of human mitochondrial leaderless mRNA translation initiation. Authors: Shuangjie Shen / Yinghua Xu / Daniel L Kober / Jinfan Wang / ![]() Abstract: Mitochondrial translation is essential for cellular function, and its dysregulation is associated with mitochondrial disorders and cancer. However, the mechanisms by which human mitochondrial ...Mitochondrial translation is essential for cellular function, and its dysregulation is associated with mitochondrial disorders and cancer. However, the mechanisms by which human mitochondrial ribosomes initiate translation remain poorly understood, particularly because mitochondrial mRNAs generally lack the 5' untranslated regions that guide translation initiation in bacterial and cytoplasmic systems. Using real-time single-molecule fluorescence measurements, biochemical assays, and cryo-EM analysis, we show that human mitochondrial translation initiation occurs through two parallel pathways. In one pathway, leaderless mRNA first loads onto the 28S small subunit, followed by recruitment of the 39S large subunit to form the 55S initiation complex. In the second pathway, a preassembled 55S monosome directly loads onto leaderless mRNA. Both pathways require recruitment of mtIF2 and fMet-tRNA before mRNA binding. However, the monosome-loading pathway tolerates non-formylated Met-tRNA and is suppressed by mtIF3. Together, these findings define the heterogeneous pathways of human mitochondrial translation initiation on leaderless mRNAs. | ||||||||||||||||||||||||
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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 | 9ojm.cif.gz | 1.8 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9ojm.ent.gz | 1.4 MB | Display | PDB format |
| PDBx/mmJSON format | 9ojm.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/oj/9ojm ftp://data.pdbj.org/pub/pdb/validation_reports/oj/9ojm | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 70544MC C: citing same article ( M: map data used to model this data |
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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
-Small ribosomal subunit protein ... , 18 types, 18 molecules 0134BGHILMNRTUVWXZ
| #1: Protein | Mass: 25336.084 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P82930 |
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| #2: Protein | Mass: 32156.938 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P82673 |
| #4: Protein | Mass: 8936.875 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9NWT8 |
| #5: Protein | Mass: 70984.156 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q96EY7 |
| #10: Protein | Mass: 25988.881 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9Y399 |
| #15: Protein | Mass: 40136.102 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P82933 |
| #16: Protein | Mass: 16360.981 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P82664 |
| #17: Protein | Mass: 14509.841 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P82912 |
| #20: Protein | Mass: 20729.482 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P82914 |
| #21: Protein | Mass: 13438.712 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9Y3D3 |
| #22: Protein | Mass: 12349.650 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9Y2R5 |
| #26: Protein | Mass: 34251.141 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P82650 |
| #28: Protein | Mass: 19585.846 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P82663 |
| #29: Protein | Mass: 21183.117 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9BYN8 |
| #30: Protein | Mass: 43969.762 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q92552 |
| #31: Protein | Mass: 11263.965 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9Y2Q9 |
| #32: Protein | Mass: 40421.258 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)References: UniProt: P51398, Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement |
| #34: Protein | Mass: 11952.871 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9Y291 |
-Protein , 2 types, 2 molecules 27
| #3: Protein | Mass: 13498.819 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q96BP2 |
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| #8: Protein | Mass: 63169.180 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P46199 |
-RNA chain , 3 types, 3 molecules 56A
| #6: RNA chain | Mass: 22664.498 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: GenBank: 1896813686 |
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| #7: RNA chain | Mass: 1241.786 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) |
| #9: RNA chain | Mass: 306547.531 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: GenBank: 1858621102 |
-28S ribosomal protein ... , 11 types, 11 molecules CDEFJKOPQSY
| #11: Protein | Mass: 15333.757 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q96EL2 |
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| #12: Protein | Mass: 38919.043 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P82675 |
| #13: Protein | Mass: 13861.032 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P82932 |
| #14: Protein | Mass: 24569.783 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9Y2R9 |
| #18: Protein | Mass: 12013.163 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O15235 |
| #19: Protein | Mass: 12282.349 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O60783 |
| #23: Protein | Mass: 22573.775 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) |
| #24: Protein | Mass: 11188.229 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) |
| #25: Protein | Mass: 10764.652 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P82921 |
| #27: Protein | Mass: 15702.971 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) |
| #33: Protein | Mass: 17631.842 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) |
-Non-polymers , 8 types, 1497 molecules 














| #35: Chemical | ChemComp-MG / #36: Chemical | ChemComp-K / #37: Chemical | ChemComp-GTP / | #38: Chemical | ChemComp-ZN / | #39: Chemical | #40: Chemical | ChemComp-GDP / | #41: Chemical | ChemComp-ATP / | #42: Water | ChemComp-HOH / | |
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-Details
| Has ligand of interest | N |
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| Has protein modification | N |
-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 mitochondrial 28S PIC with tRNA and mtIF2 / Type: RIBOSOME / Entity ID: #1-#34 / 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 |
| 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: 2500 nm / Nominal defocus min: 1200 nm |
| Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||
| 3D reconstruction | Resolution: 2.5 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 107666 / Symmetry type: POINT | ||||||||||||
| Atomic model building | Protocol: RIGID BODY FIT |
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About Yorodumi




Homo sapiens (human)
United States, 4items
Citation

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FIELD EMISSION GUN