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Open data
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Basic information
| Entry | Database: PDB / ID: 9o17 | ||||||||||||
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| Title | Cryo-EM structure of Methanosarcina acetivorans 70S ribosome | ||||||||||||
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Keywords | RIBOSOME / Archaea / Methanosarcina acetivorans / 70S ribosome | ||||||||||||
| Function / homology | Function and homology informationribonuclease P activity / tRNA 5'-leader removal / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / ribosomal large subunit biogenesis / maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / maturation of SSU-rRNA / ribosome biogenesis / ribosomal small subunit biogenesis / ribosomal small subunit assembly / small ribosomal subunit ...ribonuclease P activity / tRNA 5'-leader removal / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / ribosomal large subunit biogenesis / maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / maturation of SSU-rRNA / ribosome biogenesis / ribosomal small subunit biogenesis / ribosomal small subunit assembly / small ribosomal subunit / 5S rRNA binding / ribosomal large subunit assembly / small ribosomal subunit rRNA binding / large ribosomal subunit rRNA binding / cytosolic small ribosomal subunit / cytosolic large ribosomal subunit / cytoplasmic translation / tRNA binding / negative regulation of translation / rRNA binding / structural constituent of ribosome / ribosome / translation / ribonucleoprotein complex / mRNA binding / RNA binding / zinc ion binding / cytoplasm / cytosol Similarity search - Function | ||||||||||||
| Biological species | Methanosarcina acetivorans (archaea) | ||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.92 Å | ||||||||||||
Authors | Ghosh, A. / Fordjour, G.N.R. / Armache, J.-P. / Ferry, J.G. / Murakami, K.S. / Bevilacqua, P.C. | ||||||||||||
| Funding support | United States, 3items
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Citation | Journal: J Biol Chem / Year: 2025Title: Cryo-EM study and in vivo chemical mapping of the Methanosarcina acetivorans ribosome and its dimerization via a repurposed enzyme and translation factor. Authors: George N R Fordjour / Anwesha Ghosh / James G Ferry / Jean-Paul Armache / Philip C Bevilacqua / Katsuhiko S Murakami / ![]() Abstract: Despite the overall conservation of ribosomes across all domains of life, differences in their 3D architecture, rRNA sequences, ribosomal protein composition, and translation factor requirements ...Despite the overall conservation of ribosomes across all domains of life, differences in their 3D architecture, rRNA sequences, ribosomal protein composition, and translation factor requirements reflect lineage-specific adaptations to environmental niches. In the domain Archaea, structural studies have primarily focused on nonmethanogenic thermophiles and halophiles, leaving it unclear whether these represent the broader Archaea domain. Here, we report the cryo-electron microscopy (cryo-EM) structure of the ribosome from Methanosarcina acetivorans, a previously unreported high-resolution structure from a model mesophilic methanogenic archaeon. Compared to ribosomes from extremophiles, the M. acetivorans ribosome has a simplified architecture, lacking paralogous duplications and containing a reduced complement of ribosomal proteins. Structures of the large subunit (50S) from cells grown with either methanol or acetate show conserved rRNA folding and protein composition. High-resolution structures of the 50S subunit from the two growth substrates enabled us to investigate structural properties that may influence in vivo dimethyl sulfate reactivity, an orthogonal chemical approach used to probe RNA structure. We observed good agreement between in vivo dimethyl sulfate reactivity and ribosome structure. Finally, we identify a previously uncharacterized ribosome dimerization mode involving only 50S subunits and mediated by a heterotetrameric complex of PurH and aEF2-proteins with alternative metabolic and translational roles. This macromolecular assembly, which we term the methanogen ribosome dimerization factor, likely mediates ribosome hibernation, revealing an alternative regulatory mechanism in translation. | ||||||||||||
| 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 | 9o17.cif.gz | 5.3 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9o17.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9o17.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 9o17_validation.pdf.gz | 2.3 MB | Display | wwPDB validaton report |
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| Full document | 9o17_full_validation.pdf.gz | 2.7 MB | Display | |
| Data in XML | 9o17_validation.xml.gz | 303.4 KB | Display | |
| Data in CIF | 9o17_validation.cif.gz | 490.6 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/o1/9o17 ftp://data.pdbj.org/pub/pdb/validation_reports/o1/9o17 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 49998MC ![]() 9nriC ![]() 9ntaC ![]() 9ou7C 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 , 3 types, 3 molecules AABABB
| #1: RNA chain | Mass: 478373.938 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Methanosarcina acetivorans (archaea) / References: GenBank: 470466243 |
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| #26: RNA chain | Mass: 937667.750 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Methanosarcina acetivorans (archaea) / References: GenBank: 19918815 |
| #27: RNA chain | Mass: 41399.551 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Methanosarcina acetivorans (archaea) / References: GenBank: 19918815 |
+Small ribosomal subunit protein ... , 24 types, 24 molecules ABACADAEAFAGAIAJAKALANAOAPARAQASAUAVAWAXAYAHAMAT
+Large ribosomal subunit protein ... , 30 types, 30 molecules BCBDBEBFBGBHBIBJBKBLBMBNBOBPBQBRBSBTBUBVBWBXBYBZBaBbBcBdBeBf
-Protein , 1 types, 1 molecules AZ
| #58: Protein | Mass: 6162.260 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Methanosarcina acetivorans (archaea) / References: UniProt: A0A832S8D7 |
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-Non-polymers , 2 types, 60 molecules 


| #59: Chemical | ChemComp-MG / #60: Chemical | ChemComp-ZN / |
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-Details
| Has ligand of interest | N |
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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: Methanosarcina acetivorans 70S ribosome / Type: RIBOSOME / Entity ID: #1-#58 / Source: NATURAL | |||||||||||||||||||||||||
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| Source (natural) | Organism: Methanosarcina acetivorans (archaea) | |||||||||||||||||||||||||
| Buffer solution | pH: 7.5 | |||||||||||||||||||||||||
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| Specimen | Conc.: 0.5 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | |||||||||||||||||||||||||
| Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277.15 K |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Talos Arctica / Image courtesy: FEI Company |
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| Microscopy | Model: FEI TALOS ARCTICA |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2000 nm / Nominal defocus min: 600 nm |
| Image recording | Electron dose: 50 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k) |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||||||||||||||||||
| 3D reconstruction | Resolution: 2.92 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 91385 / Symmetry type: POINT | ||||||||||||||||||||||||||||||||||||||||||||
| Refinement | Cross valid method: NONE Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2 | ||||||||||||||||||||||||||||||||||||||||||||
| Displacement parameters | Biso mean: 64.45 Å2 | ||||||||||||||||||||||||||||||||||||||||||||
| Refine LS restraints |
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Methanosarcina acetivorans (archaea)
United States, 3items
Citation






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FIELD EMISSION GUN