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Open data
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Basic information
| Entry | ![]() | |||||||||
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| Title | Structure of P. furiosus 70S ribosome in RsmB deleted strain | |||||||||
Map data | Composite cryo-EM map of P. furiosus 70S RsmB deleted strain | |||||||||
Sample |
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Keywords | RNA modification / cryo-EM / 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 / rRNA processing / large ribosomal subunit / ribosomal small subunit biogenesis / ribosomal small subunit assembly ...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 / rRNA processing / large ribosomal subunit / 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 | ![]() Pyrococcus furiosus (archaea) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.67 Å | |||||||||
Authors | Matzov D / Georgeson J / Westhof E / Schwartz S / Shalev-Benami M | |||||||||
| Funding support | European Union, 1 items
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Citation | Journal: Cell / Year: 2025Title: Pan-modification profiling facilitates a cross-evolutionary dissection of the thermoregulated ribosomal epitranscriptome. Authors: Miguel A Garcia-Campos / Joe Georgeson / Ronit Nir / Robert Reichelt / Kristin A Fluke / Donna Matzov / Vinithra Iyer / Brett W Burkhart / Lauren Lui / Anatoly Kustanovich / Felix ...Authors: Miguel A Garcia-Campos / Joe Georgeson / Ronit Nir / Robert Reichelt / Kristin A Fluke / Donna Matzov / Vinithra Iyer / Brett W Burkhart / Lauren Lui / Anatoly Kustanovich / Felix Grünberger / Supuni Thalalla-Gamage / Shereen A Howpay-Manage / Milan Gerovac / Nicolas Alexandre / Yuko Nobe / Jakub S Nowak / Manoj Perera / Alexander Apostle / Shiyue Fang / Sebastian Glatt / Ghil Jona / Sébastien Ferreira-Cerca / Jörg Vogel / Masato Taoka / Jordan L Meier / Eric Westhof / Thomas J Santangelo / Dina Grohmann / Moran Shalev-Benami / Schraga Schwartz / ![]() Abstract: Ribosomal RNA (rRNA) constitutes the core of ribosomes and is extensively chemically modified. Technical challenges have precluded systematically dissecting rRNA modifications and their dynamics. We ...Ribosomal RNA (rRNA) constitutes the core of ribosomes and is extensively chemically modified. Technical challenges have precluded systematically dissecting rRNA modifications and their dynamics. We develop Pan-Mod-seq, permitting inference of 16 distinct modifications across dozens of samples in parallel. We applied Pan-Mod-seq to RNA from 14 species spanning all domains of life, cultured under highly diverse conditions. While dynamic modifications are rare in mesophiles, in extreme hyperthermophiles, ∼50% of modifications are dynamic. We dissect the biogenesis and function of a conserved module of tandem mC-acC modifications, co-induced at high temperatures, via enzymes intrinsically regulated by temperature and required for growth at higher temperatures. Cryo-electron microscopy (cryo-EM) structures of ribosomes from wild-type (WT) and enzyme-deficient archaea reveal recurrent molecular interactions through which they confer structural stability, and biophysical studies demonstrate their synergistic thermostabilizing role. Our findings systematically dissect rRNA modification plasticity and pave the way for surveying the rRNA epitranscriptome in health and disease. | |||||||||
| History |
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_53100.map.gz | 45.8 MB | EMDB map data format | |
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| Header (meta data) | emd-53100-v30.xml emd-53100.xml | 81.6 KB 81.6 KB | Display Display | EMDB header |
| Images | emd_53100.png | 141 KB | ||
| Filedesc metadata | emd-53100.cif.gz | 15.8 KB | ||
| Others | emd_53100_additional_1.map.gz | 45.6 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-53100 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-53100 | HTTPS FTP |
-Validation report
| Summary document | emd_53100_validation.pdf.gz | 509.6 KB | Display | EMDB validaton report |
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| Full document | emd_53100_full_validation.pdf.gz | 509.2 KB | Display | |
| Data in XML | emd_53100_validation.xml.gz | 7.6 KB | Display | |
| Data in CIF | emd_53100_validation.cif.gz | 8.8 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-53100 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-53100 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9qf6MC ![]() 9qf4C ![]() 9qf5C ![]() 53077 ![]() 53078 ![]() 53079 ![]() 53080 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_53100.map.gz / Format: CCP4 / Size: 343 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | Composite cryo-EM map of P. furiosus 70S RsmB deleted strain | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.99 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Additional map: Composite cryo-EM map of P. furiosus 70S RsmB deleted strain
| File | emd_53100_additional_1.map | ||||||||||||
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| Annotation | Composite cryo-EM map of P. furiosus 70S RsmB deleted strain | ||||||||||||
| Projections & Slices |
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| Density Histograms |
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Sample components
+Entire : P. furiosus 70S
+Supramolecule #1: P. furiosus 70S
+Macromolecule #1: 16S rRNA
+Macromolecule #27: 23S rRNA
+Macromolecule #28: 5S rRNA
+Macromolecule #2: Small ribosomal subunit protein uS2
+Macromolecule #3: Small ribosomal subunit protein uS3
+Macromolecule #4: Small ribosomal subunit protein eS1
+Macromolecule #5: Small ribosomal subunit protein uS4
+Macromolecule #6: Small ribosomal subunit protein eS4
+Macromolecule #7: Small ribosomal subunit protein uS5
+Macromolecule #8: Small ribosomal subunit protein eS6
+Macromolecule #9: Small ribosomal subunit protein uS7
+Macromolecule #10: Small ribosomal subunit protein uS8
+Macromolecule #11: Small ribosomal subunit protein eS8
+Macromolecule #12: Small ribosomal subunit protein uS9
+Macromolecule #13: Small ribosomal subunit protein uS10
+Macromolecule #14: Small ribosomal subunit protein uS11
+Macromolecule #15: Small ribosomal subunit protein uS12
+Macromolecule #16: Small ribosomal subunit protein uS13
+Macromolecule #17: Small ribosomal subunit protein uS14
+Macromolecule #18: Small ribosomal subunit protein uS15
+Macromolecule #19: Small ribosomal subunit protein uS17
+Macromolecule #20: Small ribosomal subunit protein eS17
+Macromolecule #21: Small ribosomal subunit protein uS19
+Macromolecule #22: Small ribosomal subunit protein eS19
+Macromolecule #23: Small ribosomal subunit protein eS24
+Macromolecule #24: Small ribosomal subunit protein eS27
+Macromolecule #25: Small ribosomal subunit protein eS28
+Macromolecule #26: Zn-ribbon RNA-binding protein
+Macromolecule #29: Large ribosomal subunit protein uL2
+Macromolecule #30: Large ribosomal subunit protein uL3
+Macromolecule #31: Large ribosomal subunit protein uL4
+Macromolecule #32: Large ribosomal subunit protein uL5
+Macromolecule #33: Large ribosomal subunit protein uL6
+Macromolecule #34: Large ribosomal subunit protein eL8
+Macromolecule #35: Large ribosomal subunit protein uL16
+Macromolecule #36: Large ribosomal subunit protein uL13
+Macromolecule #37: Large ribosomal subunit protein uL14
+Macromolecule #38: Large ribosomal subunit protein eL14
+Macromolecule #39: Large ribosomal subunit protein uL15
+Macromolecule #40: Large ribosomal subunit protein eL15
+Macromolecule #41: Large ribosomal subunit protein uL18
+Macromolecule #42: Large ribosomal subunit protein eL18
+Macromolecule #43: Large ribosomal subunit protein eL19
+Macromolecule #44: Large ribosomal subunit protein eL21
+Macromolecule #45: Large ribosomal subunit protein uL22
+Macromolecule #46: Large ribosomal subunit protein uL23
+Macromolecule #47: Large ribosomal subunit protein uL24
+Macromolecule #48: Large ribosomal subunit protein eL24
+Macromolecule #49: Large ribosomal subunit protein uL29
+Macromolecule #50: Large ribosomal subunit protein uL30
+Macromolecule #51: Large ribosomal subunit protein eL30
+Macromolecule #52: Large ribosomal subunit protein eL31
+Macromolecule #53: Large ribosomal subunit protein eL32
+Macromolecule #54: Large ribosomal subunit protein eL34
+Macromolecule #55: Large ribosomal subunit protein eL33
+Macromolecule #56: Large ribosomal subunit protein eL37
+Macromolecule #57: Large ribosomal subunit protein eL43
+Macromolecule #58: Large ribosomal subunit protein eL39
+Macromolecule #59: Large ribosomal subunit protein eL40
+Macromolecule #60: Small ribosomal subunit protein eS32
+Macromolecule #61: Large ribosomal subunit protein eL42
+Macromolecule #62: Large ribosomal subunit protein eL20
+Macromolecule #63: C2H2-type domain-containing protein
+Macromolecule #64: ZINC ION
+Macromolecule #65: water
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 7.5 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 1.01 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.0 µm / Nominal defocus min: 0.5 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi




Keywords
Pyrococcus furiosus (archaea)
Authors
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Processing
FIELD EMISSION GUN

