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Yorodumi- PDB-9j9i: High-resolution cryo-EM structure of the Plasmodium falciparum 80... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 9j9i | |||||||||
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| Title | High-resolution cryo-EM structure of the Plasmodium falciparum 80S ribosome bound to E-tRNA | |||||||||
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Keywords | RIBOSOME / Plasmodium falciparum | |||||||||
| Function / homology | Function and homology information: / RMTs methylate histone arginines / Protein methylation / Protein hydroxylation / Translesion synthesis by REV1 / Translesion Synthesis by POLH / Regulation of TNFR1 signaling / Translesion synthesis by POLK / Translesion synthesis by POLI / Regulation of necroptotic cell death ...: / RMTs methylate histone arginines / Protein methylation / Protein hydroxylation / Translesion synthesis by REV1 / Translesion Synthesis by POLH / Regulation of TNFR1 signaling / Translesion synthesis by POLK / Translesion synthesis by POLI / Regulation of necroptotic cell death / Josephin domain DUBs / Ovarian tumor domain proteases / Metalloprotease DUBs / DNA Damage Recognition in GG-NER / Formation of Incision Complex in GG-NER / Formation of TC-NER Pre-Incision Complex / Dual incision in TC-NER / Gap-filling DNA repair synthesis and ligation in TC-NER / PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1 / ER Quality Control Compartment (ERQC) / Iron uptake and transport / L13a-mediated translational silencing of Ceruloplasmin expression / SRP-dependent cotranslational protein targeting to membrane / Formation of a pool of free 40S subunits / Formation of the ternary complex, and subsequently, the 43S complex / Ribosomal scanning and start codon recognition / GTP hydrolysis and joining of the 60S ribosomal subunit / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / PELO:HBS1L and ABCE1 dissociate a ribosome on a non-stop mRNA / ZNF598 and the Ribosome-associated Quality Trigger (RQT) complex dissociate a ribosome stalled on a no-go mRNA / Synthesis of active ubiquitin: roles of E1 and E2 enzymes / Aggrephagy / SCF-beta-TrCP mediated degradation of Emi1 / Degradation of DVL / Orc1 removal from chromatin / CDK-mediated phosphorylation and removal of Cdc6 / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis / KEAP1-NFE2L2 pathway / GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2 / GSK3B-mediated proteasomal degradation of PD-L1(CD274) / Ribosome Quality Control (RQC) complex extracts and degrades nascent peptide / UCH proteinases / Ub-specific processing proteases / Neddylation / Antigen processing: Ubiquitination & Proteasome degradation / AUF1 (hnRNP D0) binds and destabilizes mRNA / ABC-family protein mediated transport / preribosome / protein neddylation / regulation of proteolysis / endonucleolytic cleavage to generate mature 3'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / maturation of LSU-rRNA / protein-RNA complex assembly / 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) / ribosomal large subunit biogenesis / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / cytosolic ribosome / maturation of SSU-rRNA / maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / small-subunit processome / chloroplast / maintenance of translational fidelity / modification-dependent protein catabolic process / protein tag activity / rRNA processing / large ribosomal subunit / ribosomal small subunit assembly / ribosomal small subunit biogenesis / ribosome 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 / ubiquitin-dependent protein catabolic process / cytoplasmic translation / negative regulation of translation / rRNA binding / protein ubiquitination / structural constituent of ribosome / ribosome / translation / ribonucleoprotein complex / mRNA binding / ubiquitin protein ligase binding / nucleolus / mitochondrion / RNA binding / zinc ion binding / metal ion binding / nucleus / cytosol / cytoplasm Similarity search - Function | |||||||||
| Biological species | ![]() | |||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.46 Å | |||||||||
Authors | Yan, X.F. / Gao, Y.G. | |||||||||
| Funding support | Singapore, 2items
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Citation | Journal: Structure / Year: 2025Title: Antimalarial drug artemisinin stabilizes PfRACK1 binding to the ribosome. Authors: Ka Diam Go / Xin-Fu Yan / Grennady Wirjanata / Rya Ero / Samuel Pazicky / Jerzy Dziekan / Seth Tjia / Julien Lescar / Zbynek Bozdech / Yong-Gui Gao / ![]() Abstract: Artemisinin and its derivatives represent the core agents in artemisinin combination therapies that are the current frontline treatment for P. falciparum and P. vivax malaria infections. Artemisinins ...Artemisinin and its derivatives represent the core agents in artemisinin combination therapies that are the current frontline treatment for P. falciparum and P. vivax malaria infections. Artemisinins are known to bind a wide array of proteins that disrupt the parasite's cellular physiology. Here, we show that artemisinins' cytotoxic activity involves structural alteration of key P. falciparum macromolecular complexes, including the ribosome, proteasome, and T-complex. The structural analysis revealed that, following artemisinin treatment, a larger population of Pf80S ribosomes binds PfRACK1. Unlike in most eukaryotes, PfRACK1 does not interact with the C-terminal tail of the r-protein uS3 that in Plasmodium is truncated. This likely suggests an evolved role of uS3 in facilitating RACK1-mediated translational regulation, which would potentially benefit the parasite under certain conditions. Stabilization of RACK1 ribosome interaction likely contributes to artemisinins' mode of action. | |||||||||
| 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 | 9j9i.cif.gz | 4.3 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9j9i.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9j9i.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/j9/9j9i ftp://data.pdbj.org/pub/pdb/validation_reports/j9/9j9i | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 61273MC ![]() 9j9hC C: citing same article ( M: map data used to model this data |
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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 , 5 types, 5 molecules AjBCAQ
| #1: RNA chain | Mass: 1216541.250 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #3: RNA chain | Mass: 671337.500 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #5: RNA chain | Mass: 38410.859 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #8: RNA chain | Mass: 51206.461 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #49: RNA chain | Mass: 23774.059 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Small ribosomal subunit protein ... , 4 types, 4 molecules AAklAO
| #2: Protein | Mass: 15414.444 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #7: Protein | Mass: 30111.678 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #10: Protein | Mass: 29891.182 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #78: Protein | Mass: 6508.725 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
+40S ribosomal protein ... , 27 types, 27 molecules AHABACnopqstuyzADAEAIAKANmrvAJwALxAMAFAG
+60S ribosomal protein ... , 36 types, 36 molecules D0E1F2G3H4I5J6K7L8M9NaObQdReST...
-Ribosomal protein ... , 3 types, 3 molecules PcAP
| #47: Protein | Mass: 24197.660 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #48: Protein | Mass: 10571.592 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #58: Protein | Mass: 17437.662 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Protein , 1 types, 1 molecules f
| #57: Protein | Mass: 14645.169 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Large ribosomal subunit protein ... , 3 types, 3 molecules hiX
| #63: Protein | Mass: 10826.083 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #66: Protein | Mass: 12194.902 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #71: Protein | Mass: 16422.930 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Non-polymers , 2 types, 260 molecules 


| #80: Chemical | ChemComp-MG / #81: Chemical | ChemComp-ZN / |
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-Details
| Has ligand of interest | N |
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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: Plasmodium falciparum cytoplasmic ribosomes / Type: RIBOSOME / Entity ID: #1-#26, #30-#76, #27-#29, #77-#79 / Source: NATURAL |
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| Source (natural) | Organism: ![]() |
| Buffer solution | pH: 7.4 |
| 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: FEI TITAN KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: OTHER |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 1500 nm / Nominal defocus min: 500 nm |
| Image recording | Electron dose: 60 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
| CTF correction | Type: NONE |
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| 3D reconstruction | Resolution: 2.46 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 85400 / Symmetry type: POINT |
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