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Open data
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Basic information
| Entry | Database: PDB / ID: 9qf5 | ||||||
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| Title | Structure of P. furiosus 70S ribosome grown at 102deg | ||||||
Components |
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Keywords | RIBOSOME / RNA modification / cryo-EM | ||||||
| Function / homology | Function and homology informationribonuclease P activity / tRNA 5'-leader removal / ribosomal large subunit biogenesis / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / 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 / ribosomal large subunit biogenesis / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / 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 | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.84 Å | ||||||
Authors | Matzov, D. / Georgeson, J. / Westhof, E. / Schwartz, S. / Shalev-Benami, M. | ||||||
| Funding support | European Union, 1items
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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. | ||||||
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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 | 9qf5.cif.gz | 4 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9qf5.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9qf5.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 9qf5_validation.pdf.gz | 1.6 MB | Display | wwPDB validaton report |
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| Full document | 9qf5_full_validation.pdf.gz | 2.1 MB | Display | |
| Data in XML | 9qf5_validation.xml.gz | 298.7 KB | Display | |
| Data in CIF | 9qf5_validation.cif.gz | 489.6 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qf/9qf5 ftp://data.pdbj.org/pub/pdb/validation_reports/qf/9qf5 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 53099MC ![]() 9qf4C ![]() 9qf6C ![]() 53072 ![]() 53073 ![]() 53074 ![]() 53076 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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| 1 |
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Components
-RNA chain , 3 types, 3 molecules A1B1B2
| #1: RNA chain | Mass: 489213.406 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() Pyrococcus furiosus (archaea) / References: GenBank: 18980902 |
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| #27: RNA chain | Mass: 997978.375 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() Pyrococcus furiosus (archaea) |
| #28: RNA chain | Mass: 40589.266 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() Pyrococcus furiosus (archaea) |
+Small ribosomal subunit protein ... , 25 types, 25 molecules AaAbAcAdAeAfAgAhAiAjAkAlAmAnAoApAqArAsAtAuAvAwAxBh
-Protein , 2 types, 2 molecules AyBk
| #26: Protein | Mass: 6824.008 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() Pyrococcus furiosus (archaea) / References: UniProt: I6U991 |
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| #63: Protein | Mass: 7597.191 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() Pyrococcus furiosus (archaea) / References: UniProt: Q8U2K5 |
+Large ribosomal subunit protein ... , 33 types, 35 molecules BABBBCBDBEBFBGBHBIBJBKBLBMBNBOBPBQBRBSBTBUBVBWBXBYBZBaBbBcBd...
-Non-polymers , 2 types, 1500 molecules 


| #64: Chemical | ChemComp-ZN / #65: Water | ChemComp-HOH / | |
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-Details
| Has ligand of interest | Y |
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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: P. furiosus 70S / Type: RIBOSOME / Entity ID: #1-#63 / Source: NATURAL |
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| Molecular weight | Experimental value: NO |
| Source (natural) | Organism: ![]() Pyrococcus furiosus (archaea) |
| 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: 3000 nm / Nominal defocus min: 500 nm |
| Image recording | Electron dose: 1.01 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
| EM software | Name: PHENIX / Version: 1.20.1_4487: / Category: model refinement | ||||||||||||||||||||||||
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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: 37459 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refine LS restraints |
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Pyrococcus furiosus (archaea)
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FIELD EMISSION GUN