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Open data
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Basic information
| Entry | ![]() | ||||||||||||
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| Title | Methanosarcina acetivorans large (50S) subunit dimer | ||||||||||||
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Keywords | Methanosarcina acetivorans / translation / large subunit dimer / 50S dimer / dimerization / hibernation / RIBOSOME | ||||||||||||
| Function / homology | Function and homology informationphosphoribosylaminoimidazolecarboxamide formyltransferase / phosphoribosylaminoimidazolecarboxamide formyltransferase activity / IMP cyclohydrolase / IMP cyclohydrolase activity / ribonuclease P activity / tRNA 5'-leader removal / 'de novo' IMP biosynthetic process / translational elongation / translation elongation factor activity / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) ...phosphoribosylaminoimidazolecarboxamide formyltransferase / phosphoribosylaminoimidazolecarboxamide formyltransferase activity / IMP cyclohydrolase / IMP cyclohydrolase activity / ribonuclease P activity / tRNA 5'-leader removal / 'de novo' IMP biosynthetic process / translational elongation / translation elongation factor activity / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / ribosomal large subunit biogenesis / ribosome biogenesis / 5S rRNA binding / ribosomal large subunit assembly / large ribosomal subunit rRNA binding / cytosolic large ribosomal subunit / cytoplasmic translation / tRNA binding / negative regulation of translation / rRNA binding / structural constituent of ribosome / ribosome / translation / ribonucleoprotein complex / GTPase activity / mRNA binding / GTP binding / RNA binding / zinc ion binding / cytoplasm / cytosol Similarity search - Function | ||||||||||||
| Biological species | Methanosarcina acetivorans (archaea) | ||||||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.51 Å | ||||||||||||
Authors | Ghosh A / Fordjour GNR / Armache J-P / Ferry JG / Murakami KS / Bevilacqua PC | ||||||||||||
| Funding support | United States, 3 items
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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. | ||||||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_70864.map.gz | 777.1 MB | EMDB map data format | |
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| Header (meta data) | emd-70864-v30.xml emd-70864.xml | 53.6 KB 53.6 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_70864_fsc.xml | 19.9 KB | Display | FSC data file |
| Images | emd_70864.png | 78.5 KB | ||
| Filedesc metadata | emd-70864.cif.gz | 11.7 KB | ||
| Others | emd_70864_half_map_1.map.gz emd_70864_half_map_2.map.gz | 763.7 MB 763.7 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-70864 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-70864 | HTTPS FTP |
-Validation report
| Summary document | emd_70864_validation.pdf.gz | 1.4 MB | Display | EMDB validaton report |
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| Full document | emd_70864_full_validation.pdf.gz | 1.4 MB | Display | |
| Data in XML | emd_70864_validation.xml.gz | 30.1 KB | Display | |
| Data in CIF | emd_70864_validation.cif.gz | 39.8 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-70864 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-70864 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9ou7MC ![]() 9nriC ![]() 9ntaC ![]() 9o17C M: atomic model generated by this map C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_70864.map.gz / Format: CCP4 / Size: 824 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
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| Voxel size | X=Y=Z: 0.977 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: #2
| File | emd_70864_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #1
| File | emd_70864_half_map_2.map | ||||||||||||
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| Density Histograms |
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Sample components
+Entire : Methanosarcina acetivorans large (50S) subunit dimer
+Supramolecule #1: Methanosarcina acetivorans large (50S) subunit dimer
+Macromolecule #1: 23S rRNA
+Macromolecule #2: 5S rRNA
+Macromolecule #3: Large ribosomal subunit protein uL2
+Macromolecule #4: Large ribosomal subunit protein uL3
+Macromolecule #5: Large ribosomal subunit protein uL4
+Macromolecule #6: Large ribosomal subunit protein uL5
+Macromolecule #7: Large ribosomal subunit protein uL6
+Macromolecule #8: Large ribosomal subunit protein eL8
+Macromolecule #9: Large ribosomal subunit protein uL16
+Macromolecule #10: Large ribosomal subunit protein uL13
+Macromolecule #11: Large ribosomal subunit protein uL14
+Macromolecule #12: Large ribosomal subunit protein uL15
+Macromolecule #13: Large ribosomal subunit protein eL15
+Macromolecule #14: Large ribosomal subunit protein uL18
+Macromolecule #15: Large ribosomal subunit protein eL18
+Macromolecule #16: Large ribosomal subunit protein eL19
+Macromolecule #17: Large ribosomal subunit protein eL20
+Macromolecule #18: Large ribosomal subunit protein eL21
+Macromolecule #19: Large ribosomal subunit protein uL22
+Macromolecule #20: Large ribosomal subunit protein uL23
+Macromolecule #21: Large ribosomal subunit protein uL24
+Macromolecule #22: Large ribosomal subunit protein eL24
+Macromolecule #23: Large ribosomal subunit protein uL29
+Macromolecule #24: Large ribosomal subunit protein uL30
+Macromolecule #25: Large ribosomal subunit protein eL30
+Macromolecule #26: Large ribosomal subunit protein eL31
+Macromolecule #27: Large ribosomal subunit protein eL32
+Macromolecule #28: Large ribosomal subunit protein eL43
+Macromolecule #29: Large ribosomal subunit protein eL37
+Macromolecule #30: Large ribosomal subunit protein eL39
+Macromolecule #31: Large ribosomal subunit protein eL40
+Macromolecule #32: Large ribosomal subunit protein eL42
+Macromolecule #33: Bifunctional phosphoribosylaminoimidazolecarboxamide formyltransf...
+Macromolecule #34: Elongation factor 2
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Concentration | 0.5 mg/mL | |||||||||||||||
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| Buffer | pH: 7.5 Component:
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| Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277.15 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
| Microscope | FEI TALOS ARCTICA |
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| Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 50.0 e/Å2 |
| Electron beam | Acceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.6 µm |
| Experimental equipment | ![]() Model: Talos Arctica / Image courtesy: FEI Company |
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About Yorodumi




Keywords
Methanosarcina acetivorans (archaea)
Authors
United States, 3 items
Citation

















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Y (Row.)
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Processing
FIELD EMISSION GUN


