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Yorodumi- PDB-9scu: Cryo-EM structure of the Arabidopsis thaliana 60S ribosomal subunit -
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Open data
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Basic information
| Entry | Database: PDB / ID: 9scu | |||||||||||||||||||||
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| Title | Cryo-EM structure of the Arabidopsis thaliana 60S ribosomal subunit | |||||||||||||||||||||
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Keywords | RIBOSOME / Arabidopsis / CryoEM | |||||||||||||||||||||
| Function / homology | Function and homology informationroot morphogenesis / response to fungus / adaxial/abaxial pattern specification / leaf morphogenesis / response to high light intensity / plant-type cell wall / developmental process / plasmodesma / chloroplast envelope / plant-type vacuole ...root morphogenesis / response to fungus / adaxial/abaxial pattern specification / leaf morphogenesis / response to high light intensity / plant-type cell wall / developmental process / plasmodesma / chloroplast envelope / plant-type vacuole / response to UV-B / vacuole / nucleocytoplasmic transport / plastid / response to cold / maturation of LSU-rRNA / protein-RNA complex assembly / ribosomal large subunit biogenesis / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / cytosolic ribosome / chloroplast / modification-dependent protein catabolic process / protein tag activity / large ribosomal subunit / ribosome biogenesis / response to oxidative stress / 5S rRNA binding / ribosomal large subunit assembly / large ribosomal subunit rRNA binding / cytosolic large ribosomal subunit / cytoplasmic translation / negative regulation of translation / rRNA binding / protein ubiquitination / structural constituent of ribosome / ribosome / translation / ribonucleoprotein complex / cell division / mRNA binding / ubiquitin protein ligase binding / nucleolus / endoplasmic reticulum / mitochondrion / RNA binding / extracellular region / nucleoplasm / zinc ion binding / nucleus / plasma membrane / cytosol / cytoplasm Similarity search - Function | |||||||||||||||||||||
| Biological species | ![]() | |||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.9 Å | |||||||||||||||||||||
Authors | Karki, S. / Lu, X. / Paatero, A.O. / Ruonala, R. / Tranter, D. / Guryanov, S. / Rehan, S. / Hellmann, E. / Haakonsson, A. / Butcher, S.J. ...Karki, S. / Lu, X. / Paatero, A.O. / Ruonala, R. / Tranter, D. / Guryanov, S. / Rehan, S. / Hellmann, E. / Haakonsson, A. / Butcher, S.J. / Huiskonen, J.T. / Kajander, T. / Helariutta, Y. / Paavilainen, V.O. | |||||||||||||||||||||
| Funding support | United States, Finland, 2items
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Citation | Journal: Structure / Year: 2026Title: Cryo-EM structure of the Arabidopsisthaliana ribosome in translating and non-translating states. Authors: Sudeep Karki / Xun Lu / Anja O Paatero / Raili Ruonala / Dale Tranter / Sergey Guryanov / Shahid Rehan / Eva Hellmann / Anders Haakonsson / Sarah J Butcher / Juha T Huiskonen / Tommi ...Authors: Sudeep Karki / Xun Lu / Anja O Paatero / Raili Ruonala / Dale Tranter / Sergey Guryanov / Shahid Rehan / Eva Hellmann / Anders Haakonsson / Sarah J Butcher / Juha T Huiskonen / Tommi Kajander / Yrjö Helariutta / Ville O Paavilainen / ![]() Abstract: Translational control of mRNA expression underpins much of post-transcriptional gene expression driving developmental processes in eukaryotes. How ribosomal mRNA translation is executed in plants may ...Translational control of mRNA expression underpins much of post-transcriptional gene expression driving developmental processes in eukaryotes. How ribosomal mRNA translation is executed in plants may be especially important for adapting to an ever-changing environment. Arabidopsis thaliana is the main genetic model organism in plant science, yet structural insights into developmental processes where ribosomal gene expression plays important roles currently remain lacking. Here, we present cryoelectron microscopy (cryo-EM) structures of the Arabidopsis cytosolic ribosome in both translating and non-translating states, which together provide new structural details into how translation of cytosolic mRNAs is coordinated. Our structures reveal detailed information on the interactions of tRNAs, mRNA, and the nascent polypeptide with subunits of the actively translating 80S ribosome and the role of ribosomal RNA methylation in stabilizing ribosomal subunits. The structures provide a foundation for interpreting the functional effects of many mutations of ribosomal proteins affecting phenotypic effects for plant tissue development. | |||||||||||||||||||||
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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 | 9scu.cif.gz | 2.9 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9scu.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9scu.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/sc/9scu ftp://data.pdbj.org/pub/pdb/validation_reports/sc/9scu | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 54774MC ![]() 9sdpC ![]() 9sdqC 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 567
| #1: RNA chain | Mass: 1094756.250 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #9: RNA chain | Mass: 38917.082 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #13: RNA chain | Mass: 52785.336 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
+Large ribosomal subunit protein ... , 36 types, 36 molecules CkCACKClCYCLCZCMCNCawCOCBCPCcCQCCCRCdCDCTCeCVCECWCfCXCFCgCG...
-Protein , 4 types, 4 molecules CpCmCbCS
| #5: Protein | ( Mass: 10356.228 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #10: Protein | Mass: 14763.478 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #17: Protein | Mass: 9410.883 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #26: Protein | Mass: 25781.607 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Non-polymers , 3 types, 51 molecules 




| #44: Chemical | ChemComp-K / #45: Chemical | ChemComp-MG / #46: Chemical | ChemComp-ZN / | |
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-Details
| Has ligand of interest | Y |
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| Has protein modification | N |
-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: TISSUE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
| Component | Name: 60S LSU Arabidopsis (root) ribosome complex / Type: RIBOSOME Entity ID: #1, #9, #13, #3, #19, #23, #27, #31, #35, #37, #39, #41, #43, #4, #8, #12, #14, #18, #20, #22, #24, #26, #28, #30, #32, #34, #7, #11, #15, #17, #21, #25, #29, #33, #36, #38, #40, #42, #2, #6, #10, #5, #16 Source: NATURAL |
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| Molecular weight | Value: 4.3 MDa / Experimental value: NO |
| Source (natural) | Organism: ![]() |
| Buffer solution | pH: 7.4 Details: 50 mM Hepes, pH 7.4, 5 mM MgAc, 100 mM KAc, pH 7.5, 1 mM DTT, Complete protease inhibitor |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Specimen support | Grid material: COPPER / Grid type: Quantifoil |
| 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: OTHER |
| Electron lens | Mode: OTHER / Nominal magnification: 105000 X / Nominal defocus max: 1200 nm / Nominal defocus min: 600 nm / Cs: 2.7 mm |
| Image recording | Electron dose: 24.512 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
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| CTF correction | Type: NONE | ||||||||||||||||
| 3D reconstruction | Resolution: 2.9 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 115070 / Symmetry type: POINT | ||||||||||||||||
| Refinement | Highest resolution: 2.9 Å Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS) |
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FIELD EMISSION GUN