[English] 日本語
Yorodumi- PDB-9srd: Cryo-EM structure of P. abyssi 70S ribosome in complex with hiber... -
+
Open data
-
Basic information
| Entry | Database: PDB / ID: 9srd | ||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Title | Cryo-EM structure of P. abyssi 70S ribosome in complex with hibernation factor HibA (HibA-uL5 conformation) | ||||||||||||||||||||||||||||||
Components |
| ||||||||||||||||||||||||||||||
Keywords | RIBOSOME / 70S / Hibernation / Pyrococcus abyssi | ||||||||||||||||||||||||||||||
| 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 / large ribosomal subunit / ribosomal small subunit assembly / ribosome biogenesis / ribosomal small subunit biogenesis ...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 / large ribosomal subunit / ribosomal small subunit assembly / ribosome biogenesis / ribosomal small subunit biogenesis / 5S rRNA binding / ribosomal large subunit assembly / small ribosomal subunit / 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 abyssi GE5 (archaea) | ||||||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.1 Å | ||||||||||||||||||||||||||||||
Authors | Madru, C. / Bourgeois, G. / Mechulam, Y. / Schmitt, E. | ||||||||||||||||||||||||||||||
| Funding support | France, 1items
| ||||||||||||||||||||||||||||||
Citation | Journal: Nat Commun / Year: 2026Title: A family of ribosome hibernation factors widespread in Archaea. Authors: Clément Madru / Gabrielle Bourgeois / Rémi Dulermo / Régine Capeyrou / Gwendoline Joncour / Karima Figuigui / Magalie Duchateau / Julia Chamot-Rooke / Claire Duboc / Stéphane l'Haridon / ...Authors: Clément Madru / Gabrielle Bourgeois / Rémi Dulermo / Régine Capeyrou / Gwendoline Joncour / Karima Figuigui / Magalie Duchateau / Julia Chamot-Rooke / Claire Duboc / Stéphane l'Haridon / Logan Mc Teer / Marta Kwapisz / Béatrice Clouet-d'Orval / Marie Bouvier / Yves Mechulam / Guillaume Borrel / Emmanuelle Schmitt / Didier Flament / ![]() Abstract: Ribosome hibernation preserves translation machinery during stress, yet its mechanisms in Archaea remain poorly defined. Using cryo-EM analysis, we studied hibernation pathways in Pyrococcus abyssi ...Ribosome hibernation preserves translation machinery during stress, yet its mechanisms in Archaea remain poorly defined. Using cryo-EM analysis, we studied hibernation pathways in Pyrococcus abyssi stressed cells. We identified HibA, a previously unrecognized family of hibernation factors widespread in Archaea. HibA consists of a bacterial-like HPF/RaiA domain fused to a Cystathionine Beta Synthase module. Unexpectedly, HibA binds to the ribosome in three different conformations, occupying the A, P and E sites of tRNAs, as well as that of mRNA, enhancing its ability to protect the ribosome from degradation. Idle ribosomes also frequently accumulate the archaeal homolog of eukaryotic ribosome maturation protein SBDS (aSBDS), suggesting that stressed archaeal cells may engage parallel hibernation routes in which aSBDS can complement HibA. Deletion of hibA in Thermococcus barophilus delays recovery from stationary phase and reduces 70S ribosome pools, establishing its role in ribosome preservation. Taxonomic profiling shows that many archaeal lineages encode distinct repertoires of ribosome-associated protection factors, underscoring the modular and multi-layered nature of archaeal hibernation systems. In addition, a comprehensive phylogenetic analysis highlights the evolutionary relationships between prevalent ribosome hibernation factors across Bacteria and Archaea. | ||||||||||||||||||||||||||||||
| History |
|
-
Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
|---|
-
Downloads & links
-
Download
| PDBx/mmCIF format | 9srd.cif.gz | 4.2 MB | Display | PDBx/mmCIF format |
|---|---|---|---|---|
| PDB format | pdb9srd.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9srd.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/sr/9srd ftp://data.pdbj.org/pub/pdb/validation_reports/sr/9srd | HTTPS FTP |
|---|
-Related structure data
| Related structure data | ![]() 55138MC M: map data used to model this data C: citing same article ( |
|---|---|
| Similar structure data | Similarity search - Function & homology F&H Search |
-
Links
-
Assembly
| Deposited unit | ![]()
|
|---|---|
| 1 |
|
-
Components
-RNA chain , 3 types, 3 molecules 123
| #1: RNA chain | Mass: 984301.750 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() Pyrococcus abyssi GE5 (archaea) |
|---|---|
| #2: RNA chain | Mass: 492728.781 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() Pyrococcus abyssi GE5 (archaea) |
| #3: RNA chain | Mass: 41443.777 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() Pyrococcus abyssi GE5 (archaea) |
+30S ribosomal protein ... , 25 types, 26 molecules AAABADAEAFAGAHAIAJAKALAMANAPAQARASAUAVB6AWAXAYAZATAO
-Protein , 4 types, 6 molecules ACA3BGB4BkH
| #6: Protein | Mass: 7163.395 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() Pyrococcus abyssi GE5 (archaea) / References: UniProt: G8ZFK7 | ||||
|---|---|---|---|---|---|
| #29: Protein | Mass: 13442.678 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) ![]() Pyrococcus abyssi GE5 (archaea) / References: UniProt: P62008#64: Protein | | Mass: 7795.481 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() Pyrococcus abyssi GE5 (archaea) / References: UniProt: G8ZKB7#65: Protein | | Mass: 44583.812 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() Pyrococcus abyssi GE5 (archaea) / References: UniProt: Q9UYR4 |
-Protein/peptide , 1 types, 1 molecules A0
| #28: Protein/peptide | Mass: 5023.395 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() Pyrococcus abyssi GE5 (archaea) / References: UniProt: Q8U232 |
|---|
+Large ribosomal subunit protein ... , 32 types, 33 molecules BBBYBOBCB5BKBLBfBUBbBeBEBaBTBWBiBIBRBQBVBjBDBFBZBPBMBSBdBNBg...
-Non-polymers , 2 types, 257 molecules 


| #66: Chemical | ChemComp-MG / #67: Chemical | ChemComp-ZN / |
|---|
-Details
| Has ligand of interest | N |
|---|---|
| Has protein modification | Y |
-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
|---|---|
| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
-
Sample preparation
| Component | Name: Cryo-EM structure of P. abyssi 70S ribosome in complex with hibernation factor HibA (HibA-uL5 conformation) Type: RIBOSOME / Entity ID: #1-#65 / Source: NATURAL |
|---|---|
| Source (natural) | Organism: ![]() Pyrococcus abyssi GE5 (archaea) |
| Buffer solution | pH: 7.5 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Vitrification | Cryogen name: ETHANE |
-
Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
|---|---|
| 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: 800 nm / Nominal defocus min: 300 nm |
| Image recording | Electron dose: 40 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
-
Processing
| EM software |
| ||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 2.1 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 207000 / Symmetry type: POINT | ||||||||||||||||||||||||
| Atomic model building | Source name: Other / Type: other | ||||||||||||||||||||||||
| Refinement | Highest resolution: 2.1 Å Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS) | ||||||||||||||||||||||||
| Refine LS restraints |
|
Movie
Controller
About Yorodumi




Pyrococcus abyssi GE5 (archaea)
France, 1items
Citation
PDBj




































FIELD EMISSION GUN