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Yorodumi- PDB-8ipa: Wheat 80S ribosome stalled on AUG-Stop boron dependently with cyc... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 8ipa | ||||||
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| Title | Wheat 80S ribosome stalled on AUG-Stop boron dependently with cycloheximide | ||||||
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Keywords | TRANSLATION / ribosome | ||||||
| Function / homology | Function and homology informationresponse to high light intensity / translation release factor complex / cytoplasmic translational termination / translation release factor activity, codon specific / translation release factor activity / sequence-specific mRNA binding / response to UV-B / negative regulation of translational frameshifting / endonucleolytic cleavage to generate mature 3'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / protein-RNA complex assembly ...response to high light intensity / translation release factor complex / cytoplasmic translational termination / translation release factor activity, codon specific / translation release factor activity / sequence-specific mRNA binding / response to UV-B / negative regulation of translational frameshifting / endonucleolytic cleavage to generate mature 3'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / protein-RNA complex assembly / maturation of LSU-rRNA / endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / translation regulator activity / cytosolic ribosome / rescue of stalled ribosome / protein kinase C binding / 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) / small-subunit processome / rRNA processing / ribosome biogenesis / ribosome binding / ribosomal small subunit biogenesis / ribosomal small subunit assembly / small ribosomal subunit / 5S rRNA binding / large ribosomal subunit rRNA binding / cytosolic small ribosomal subunit / cytosolic large ribosomal subunit / cytoplasmic translation / negative regulation of translation / rRNA binding / structural constituent of ribosome / ribosome / translation / ribonucleoprotein complex / mRNA binding / mitochondrion / RNA binding / zinc ion binding / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
| Biological species | ![]() ![]() | ||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.4 Å | ||||||
Authors | Yokoyama, T. / Tanaka, M. / Saito, H. / Nishimoto, M. / Tsuda, K. / Sotta, N. / Shigematsu, H. / Shirouzu, M. / Iwasaki, S. / Ito, T. / Fujiwara, T. | ||||||
| Funding support | Japan, 1items
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Citation | Journal: Nat Chem Biol / Year: 2024Title: Boric acid intercepts 80S ribosome migration from AUG-stop by stabilizing eRF1. Authors: Mayuki Tanaka / Takeshi Yokoyama / Hironori Saito / Madoka Nishimoto / Kengo Tsuda / Naoyuki Sotta / Hideki Shigematsu / Mikako Shirouzu / Shintaro Iwasaki / Takuhiro Ito / Toru Fujiwara / ![]() Abstract: In response to environmental changes, cells flexibly and rapidly alter gene expression through translational controls. In plants, the translation of NIP5;1, a boric acid diffusion facilitator, is ...In response to environmental changes, cells flexibly and rapidly alter gene expression through translational controls. In plants, the translation of NIP5;1, a boric acid diffusion facilitator, is downregulated in response to an excess amount of boric acid in the environment through upstream open reading frames (uORFs) that consist of only AUG and stop codons. However, the molecular details of how this minimum uORF controls translation of the downstream main ORF in a boric acid-dependent manner have remained unclear. Here, by combining ribosome profiling, translation complex profile sequencing, structural analysis with cryo-electron microscopy and biochemical assays, we show that the 80S ribosome assembled at AUG-stop migrates into the subsequent RNA segment, followed by downstream translation initiation, and that boric acid impedes this process by the stable confinement of eukaryotic release factor 1 on the 80S ribosome on AUG-stop. Our results provide molecular insight into translation regulation by a minimum and environment-responsive uORF. | ||||||
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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 | 8ipa.cif.gz | 4.5 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb8ipa.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 8ipa.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 8ipa_validation.pdf.gz | 2.3 MB | Display | wwPDB validaton report |
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| Full document | 8ipa_full_validation.pdf.gz | 2.4 MB | Display | |
| Data in XML | 8ipa_validation.xml.gz | 342.4 KB | Display | |
| Data in CIF | 8ipa_validation.cif.gz | 589.6 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ip/8ipa ftp://data.pdbj.org/pub/pdb/validation_reports/ip/8ipa | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 35637MC ![]() 8ip8C ![]() 8ip9C ![]() 8ipbC 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 , 6 types, 6 molecules aaRBSBTBalcl
| #1: RNA chain | Mass: 583613.562 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #75: RNA chain | Mass: 1095659.000 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #76: RNA chain | Mass: 51535.613 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #77: RNA chain | Mass: 38716.957 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #78: RNA chain | Mass: 2229.403 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #80: RNA chain | Mass: 24446.926 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
+40S ribosomal protein ... , 31 types, 31 molecules bacadagaiajakalamanaoapaqarasatauavawaxayazabbcbdbebfbgbhbibAA
-Protein , 2 types, 2 molecules habl
| #6: Protein | Mass: 36200.527 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #79: Protein | Mass: 49051.281 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
+60S ribosomal protein ... , 41 types, 41 molecules BACADAEAFAGAHAIAJAKALAMANAOAPAQARASATAUAVAWAXAYAZAABBBCBDBEB...
-Non-polymers , 3 types, 289 molecules 




| #81: Chemical | ChemComp-MG / #82: Chemical | ChemComp-ZN / #83: Chemical | ChemComp-3HE / | |
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-Details
| Has ligand of interest | N |
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-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: Wheat 80S ribosome stalled on AUG-Stop boron dependently with cycloheximide Type: RIBOSOME / Entity ID: #1-#80 / Source: NATURAL |
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| Molecular weight | Experimental value: NO |
| Source (natural) | Organism: ![]() |
| Buffer solution | pH: 7 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Specimen support | Grid material: COPPER / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R1.2/1.3 |
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Talos Arctica / Image courtesy: FEI Company |
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| Microscopy | Model: FEI TECNAI ARCTICA |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal magnification: 23500 X / Nominal defocus max: 3500 nm / Nominal defocus min: 500 nm / Cs: 2.7 mm |
| Specimen holder | Cryogen: NITROGEN / Specimen holder model: OTHER |
| Image recording | Electron dose: 40 e/Å2 / Detector mode: SUPER-RESOLUTION / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 69380 / Symmetry type: POINT |
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Japan, 1items
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FIELD EMISSION GUN