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Yorodumi- PDB-9krp: Structure of the HCV IRES-dependent 48S translation initiation co... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 9krp | |||||||||
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| Title | Structure of the HCV IRES-dependent 48S translation initiation complex with eIF5B and eIF3 | |||||||||
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Keywords | RIBOSOME / HCV IRES | |||||||||
| Function / homology | Function and homology informationpositive regulation of mRNA binding / viral translational termination-reinitiation / eukaryotic translation initiation factor 3 complex, eIF3e / cap-dependent translational initiation / eukaryotic translation initiation factor 3 complex, eIF3m / IRES-dependent viral translational initiation / translation reinitiation / formation of cytoplasmic translation initiation complex / eukaryotic translation initiation factor 3 complex / multi-eIF complex ...positive regulation of mRNA binding / viral translational termination-reinitiation / eukaryotic translation initiation factor 3 complex, eIF3e / cap-dependent translational initiation / eukaryotic translation initiation factor 3 complex, eIF3m / IRES-dependent viral translational initiation / translation reinitiation / formation of cytoplasmic translation initiation complex / eukaryotic translation initiation factor 3 complex / multi-eIF complex / cytoplasmic translational initiation / eukaryotic 43S preinitiation complex / mRNA cap binding / eukaryotic 48S preinitiation complex / negative regulation of endoplasmic reticulum unfolded protein response / oxidized pyrimidine DNA binding / response to TNF agonist / positive regulation of base-excision repair / positive regulation of respiratory burst involved in inflammatory response / positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage / positive regulation of gastrulation / protein tyrosine kinase inhibitor activity / positive regulation of endodeoxyribonuclease activity / IRE1-RACK1-PP2A complex / nucleolus organization / positive regulation of Golgi to plasma membrane protein transport / TNFR1-mediated ceramide production / negative regulation of DNA repair / negative regulation of RNA splicing / protein-synthesizing GTPase / metal-dependent deubiquitinase activity / nuclear-transcribed mRNA catabolic process, nonsense-mediated decay / supercoiled DNA binding / neural crest cell differentiation / regulation of translational initiation / NF-kappaB complex / cysteine-type endopeptidase activator activity involved in apoptotic process / oxidized purine DNA binding / positive regulation of ubiquitin-protein transferase activity / negative regulation of intrinsic apoptotic signaling pathway in response to hydrogen peroxide / regulation of establishment of cell polarity / negative regulation of bicellular tight junction assembly / ubiquitin-like protein conjugating enzyme binding / negative regulation of phagocytosis / rRNA modification in the nucleus and cytosol / erythrocyte homeostasis / Formation of the ternary complex, and subsequently, the 43S complex / cytoplasmic side of rough endoplasmic reticulum membrane / laminin receptor activity / negative regulation of ubiquitin protein ligase activity / protein kinase A binding / ion channel inhibitor activity / Ribosomal scanning and start codon recognition / pigmentation / Translation initiation complex formation / positive regulation of mitochondrial depolarization / positive regulation of T cell receptor signaling pathway / fibroblast growth factor binding / negative regulation of Wnt signaling pathway / monocyte chemotaxis / positive regulation of activated T cell proliferation / negative regulation of translational frameshifting / TOR signaling / Protein hydroxylation / BH3 domain binding / SARS-CoV-1 modulates host translation machinery / iron-sulfur cluster binding / regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway / regulation of cell division / cellular response to ethanol / mTORC1-mediated signalling / Peptide chain elongation / Selenocysteine synthesis / Formation of a pool of free 40S subunits / positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator / endonucleolytic cleavage to generate mature 3'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / Eukaryotic Translation Termination / ubiquitin ligase inhibitor activity / positive regulation of GTPase activity / SRP-dependent cotranslational protein targeting to membrane / Response of EIF2AK4 (GCN2) to amino acid deficiency / protein serine/threonine kinase inhibitor activity / negative regulation of ubiquitin-dependent protein catabolic process / positive regulation of signal transduction by p53 class mediator / Viral mRNA Translation / negative regulation of respiratory burst involved in inflammatory response / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / GTP hydrolysis and joining of the 60S ribosomal subunit / L13a-mediated translational silencing of Ceruloplasmin expression / Major pathway of rRNA processing in the nucleolus and cytosol / phagocytic cup / regulation of translational fidelity / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / negative regulation of protein binding / Protein methylation / positive regulation of intrinsic apoptotic signaling pathway / Nuclear events stimulated by ALK signaling in cancer / spindle assembly / laminin binding / rough endoplasmic reticulum Similarity search - Function | |||||||||
| Biological species | Homo sapiens (human) Hepacivirus hominis | |||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.2 Å | |||||||||
Authors | Iwasaki, W. / Kashiwagi, K. / Sakamoto, A. / Nishimoto, M. / Takahashi, M. / Machida, K. / Imataka, H. / Matsumoto, A. / Shichino, Y. / Iwasaki, S. ...Iwasaki, W. / Kashiwagi, K. / Sakamoto, A. / Nishimoto, M. / Takahashi, M. / Machida, K. / Imataka, H. / Matsumoto, A. / Shichino, Y. / Iwasaki, S. / Imami, K. / Ito, T. | |||||||||
| Funding support | Japan, 2items
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Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2025Title: Structural Insights into the Role of eIF3 in Translation Mediated by the HCV IRES Authors: Iwasaki, W. / Kashiwagi, K. / Sakamoto, A. / Nishimoto, M. / Takahashi, M. / Machida, K. / Imataka, H. / Matsumoto, A. / Shichino, Y. / Iwasaki, S. / Imami, K. / Ito, T. | |||||||||
| History |
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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 | 9krp.cif.gz | 2.6 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9krp.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9krp.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 9krp_validation.pdf.gz | 1.9 MB | Display | wwPDB validaton report |
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| Full document | 9krp_full_validation.pdf.gz | 2 MB | Display | |
| Data in XML | 9krp_validation.xml.gz | 242.9 KB | Display | |
| Data in CIF | 9krp_validation.cif.gz | 410.5 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/kr/9krp ftp://data.pdbj.org/pub/pdb/validation_reports/kr/9krp | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 62535MC ![]() 9kkfC ![]() 9kn5C ![]() 9kn6C ![]() 9kzuC ![]() 9kzxC 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
-Protein , 4 types, 4 molecules SAshSg5B
| #1: Protein | Mass: 32883.938 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P08865 |
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| #32: Protein | Mass: 18004.041 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62979 |
| #33: Protein | Mass: 35115.652 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P63244 |
| #38: Protein | Mass: 70093.391 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: EIF5B, IF2, KIAA0741 / Cell line (production host): HEK293 / Production host: Homo sapiens (human) / References: UniProt: O60841, protein-synthesizing GTPase |
+40S ribosomal protein ... , 30 types, 30 molecules SBSCSDSESFSGSHSISJSKSLSfSNSOSPSQSRSSSTSUSVSWSXSYSZSaSbScSdSe
-RNA chain , 3 types, 3 molecules zyS2zz
| #34: RNA chain | Mass: 24231.510 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: GenBank: 174924 |
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| #36: RNA chain | Mass: 602777.875 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: GenBank: 2795772166 |
| #37: RNA chain | Mass: 107002.117 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Hepacivirus hominis / References: GenBank: 221513 |
-Protein/peptide , 1 types, 1 molecules Ln
| #35: Protein/peptide | Mass: 3473.451 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62945 |
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-Eukaryotic translation initiation factor 3 subunit ... , 9 types, 9 molecules 3m3f3a3e3c3h3d3k3l
| #39: Protein | Mass: 42555.832 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q7L2H7 |
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| #40: Protein | Mass: 37593.645 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O00303, ubiquitinyl hydrolase 1 |
| #41: Protein | Mass: 166903.781 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q14152 |
| #42: Protein | Mass: 52281.633 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P60228 |
| #43: Protein | Mass: 105503.945 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q99613 |
| #44: Protein | Mass: 39979.277 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O15372 |
| #45: Protein | Mass: 64060.758 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O15371 |
| #46: Protein | Mass: 25083.619 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9UBQ5 |
| #47: Protein | Mass: 66803.734 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9Y262 |
-Non-polymers , 3 types, 12 molecules 




| #48: Chemical | | #49: Chemical | ChemComp-MG / #50: Chemical | ChemComp-GTP / | |
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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: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
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| Source (natural) |
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| Source (recombinant) | Organism: Homo sapiens (human) | ||||||||||||||||||||||||||||||
| Buffer solution | pH: 7.5 | ||||||||||||||||||||||||||||||
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||||||||||||
| Vitrification | Instrument: FEI VITROBOT MARK IV / 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: 1500 nm |
| Image recording | Electron dose: 56.2 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
| EM software | Name: PHENIX / Version: 1.21.2_5419 / Category: model refinement |
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| CTF correction | Type: NONE |
| 3D reconstruction | Resolution: 3.2 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 24895 / Symmetry type: POINT |
| Refinement | Cross valid method: NONE |
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About Yorodumi



Homo sapiens (human)
Hepacivirus hominis
Japan, 2items
Citation










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