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Yorodumi- PDB-28jw: Structure of the Chlamydomonas reinhardtii chlororibosome with P-... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 28jw | |||||||||||||||
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| Title | Structure of the Chlamydomonas reinhardtii chlororibosome with P-site tRNA | |||||||||||||||
Components |
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Keywords | RIBOSOME / chloroplast / translation / chlororibosome | |||||||||||||||
| Function / homology | Function and homology informationmitochondrial large ribosomal subunit / mitochondrial small ribosomal subunit / mitochondrial translation / plastid / chloroplast / large ribosomal subunit / transferase activity / ribosomal small subunit biogenesis / 5S rRNA binding / small ribosomal subunit ...mitochondrial large ribosomal subunit / mitochondrial small ribosomal subunit / mitochondrial translation / plastid / chloroplast / large ribosomal subunit / transferase activity / ribosomal small subunit biogenesis / 5S rRNA binding / small ribosomal subunit / ribosomal large subunit assembly / small ribosomal subunit rRNA binding / cytosolic small ribosomal subunit / large ribosomal subunit rRNA binding / cytosolic large ribosomal subunit / negative regulation of translation / rRNA binding / structural constituent of ribosome / ribosome / translation / ribonucleoprotein complex / response to antibiotic / mRNA binding / mitochondrion / RNA binding / cytoplasm Similarity search - Function | |||||||||||||||
| Biological species | ![]() | |||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.84 Å | |||||||||||||||
Authors | Waltz, F. / Kater, L. / Engel, B.D. | |||||||||||||||
| Funding support | Switzerland, 2items
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Citation | Journal: bioRxiv / Year: 2026Title: Chloroplast-encoded small subunit extensions reshape the Chlamydomonas chlororibosome. Authors: Florent Waltz / Philippe A Lehner / Philippe Van der Stappen / Lukas Kater / Stefan Pfeffer / Benjamin D Engel / ![]() Abstract: Chloroplast ribosomes (chlororibosomes) synthesize the core protein components of the photosynthetic apparatus, yet their structural diversity outside flowering plants remains largely unexplored. ...Chloroplast ribosomes (chlororibosomes) synthesize the core protein components of the photosynthetic apparatus, yet their structural diversity outside flowering plants remains largely unexplored. Here, we combine in situ cryo-electron tomography (cryo-ET) with single-particle cryo-electron microscopy (cryo-EM) to determine the structure of the chlororibosome from the unicellular green alga . Subtomogram averaging of chlororibosomes in their native environment, resolved to ~5 Å resolution and in distinct translational states, reveals particles both free in the stroma and loosely tethered to thylakoid membranes. These reconstructions uncover an additional "arm" domain on the small subunit. High-resolution single-particle reconstruction of isolated chlororibosomes to ~2.5 Å, in states bound either to the inhibitory translation factor pY or to a nascent chain-linked P-site tRNA, reveals that this domain is built primarily from extensive chloroplast-encoded insertions and extensions of conserved small subunit proteins, supported by chlororibosome-specific ribosomal proteins. The arm domain is located around the mRNA entry and exit channels, suggesting a role in stabilizing the mRNA trajectory through the small subunit and organizing chloroplast polysomes. Together, these data reveal unexpected structural variation of algal chlororibosomes and suggest that chloroplast translation has diversified substantially even among relatively closely related photosynthetic lineages. | |||||||||||||||
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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 | 28jw.cif.gz | 4 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb28jw.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 28jw.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/8j/28jw ftp://data.pdbj.org/pub/pdb/validation_reports/8j/28jw | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 56567MC ![]() 28luC ![]() 9tvuC 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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| 1 |
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Components
+Protein , 22 types, 22 molecules 067FHJLPRTUVXZafmtuxwe
-RNA chain , 8 types, 8 molecules 3514yxx2A
| #2: RNA chain | Mass: 38858.949 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #3: RNA chain | Mass: 15149.069 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #33: RNA chain | Mass: 769308.625 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #34: RNA chain | Mass: 88325.664 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #35: RNA chain | Mass: 24565.742 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #36: RNA chain | Mass: 380.567 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #57: RNA chain | Mass: 476372.562 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #62: RNA chain | Mass: 1884.197 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-50S ribosomal protein ... , 2 types, 2 molecules 8Y
| #6: Protein | Mass: 12106.231 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #32: Protein | Mass: 14777.946 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Large ribosomal subunit protein ... , 14 types, 14 molecules 9BCDEGIKMNOQSW
| #7: Protein/peptide | Mass: 4273.327 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #8: Protein | Mass: 30955.770 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #9: Protein | Mass: 27878.426 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #10: Protein | Mass: 25659.525 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #11: Protein | Mass: 20267.668 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #13: Protein | Mass: 22043.705 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #15: Protein | Mass: 18562.955 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #17: Protein | Mass: 13466.755 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #19: Protein | Mass: 15500.425 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #20: Protein | Mass: 19188.451 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #21: Protein | Mass: 15818.282 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #23: Protein | Mass: 13578.073 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #25: Protein | Mass: 18959.348 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #29: Protein | Mass: 21945.557 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Small ribosomal subunit protein ... , 13 types, 13 molecules dghjklnqrsbci
| #38: Protein | Mass: 30082.121 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #40: Protein | Mass: 19163.799 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #41: Protein | Mass: 15916.647 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #42: Protein | Mass: 18736.729 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #43: Protein | Mass: 14260.867 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #44: Protein | Mass: 14637.429 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #46: Protein | Mass: 11776.143 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #49: Protein | Mass: 11767.698 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #50: Protein | Mass: 16315.782 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #51: Protein | Mass: 10463.467 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #58: Protein | Mass: 102698.477 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #59: Protein | Mass: 82015.938 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #61: Protein | Mass: 21062.168 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-30S ribosomal protein ... , 3 types, 3 molecules opv
| #47: Protein | Mass: 15817.261 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #48: Protein | Mass: 14474.052 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #54: Protein | Mass: 33397.238 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Non-polymers , 3 types, 450 molecules 




| #63: Chemical | ChemComp-MG / #64: Chemical | ChemComp-K / #65: Chemical | ChemComp-CLM / | |
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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: Chloroplast ribosome / Type: RIBOSOME / Source: NATURAL |
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| Molecular weight | Experimental value: NO |
| Source (natural) | Organism: ![]() |
| Buffer solution | pH: 7.5 |
| Specimen | Conc.: 2.5 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Specimen support | Grid material: COPPER / Grid type: Quantifoil R2/1 |
| Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % |
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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 magnification: 75000 X / Nominal defocus max: 2000 nm / Nominal defocus min: 800 nm |
| Image recording | Electron dose: 40 e/Å2 / Film or detector model: TFS FALCON 4i (4k x 4k) |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||||||
| 3D reconstruction | Resolution: 2.84 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 49141 / Algorithm: BACK PROJECTION / Symmetry type: POINT | ||||||||||||||||||||||||||||||||
| EM volume selection | Method: Template matching / Num. of tomograms: 129 / Num. of volumes extracted: 20883 | ||||||||||||||||||||||||||||||||
| Refinement | Highest resolution: 2.84 Å Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS) | ||||||||||||||||||||||||||||||||
| Refine LS restraints |
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