9V26
Cryo- EM structure of 75S ribosome with A/P- & P/E- tRNAs from Entamoeba histolytica bound to antibiotic paromomycin
This is a non-PDB format compatible entry.
Summary for 9V26
| Entry DOI | 10.2210/pdb9v26/pdb |
| EMDB information | 64718 |
| Descriptor | 25S rRNA, 60S ribosomal protein L7a, 60S ribosomal protein L9, putative, ... (75 entities in total) |
| Functional Keywords | 75s ribosome-par complex, a/p-trna, p/e-trna, entamoeba histolytica, ribosome |
| Biological source | Entamoeba histolytica HM-1:IMSS More |
| Total number of polymer chains | 74 |
| Total formula weight | 3174411.38 |
| Authors | Sharma, S.,Mishra, S.,Gourinath, S.,Kaushal, P.S. (deposition date: 2025-05-19, release date: 2025-10-08) |
| Primary citation | Sharma, S.,Mishra, S.,Gourinath, S.,Kaushal, P.S. Cryo-EM structure of ribosome from pathogenic protozoa Entamoeba histolytica reveals unique features of its architecture. Nat Commun, 16:7758-7758, 2025 Cited by PubMed Abstract: Entamoeba histolytica, an anaerobic protozoan parasite, is the causative agent of amoebiasis, bloody diarrhea, and liver abscesses in humans. Amoebiasis is more predominant in tropical areas with poor sanitation conditions, and it remains the fourth leading cause of death due to a protozoan infection. E. histolytica life cycle spans between an infective 'cyst stage' and an active disease-causing 'trophozoite stage'. We have isolated ribosomes from the trophozoite stage of E. histolytica. Here, we report single particle cryo-EM structures of the 53S ribosome large subunit (LSU), and 75S associated ribosomes, with P-tRNA, A/P and P/E tRNAs, and with paromomycin antibiotic, at 2.8 Å to 3.4 Å resolution. The E. histolytica possesses a reduced ribosome with a conserved core, and the periphery evolved with species-specific unique features. The most notable features are the presence of the rRNA triple helix near the peptide exit tunnel, the expansion segment H88ES102 near the exit site on LSU, and unique insertions in r-proteins. Furthermore, the 75S ribosome paromomycin complex structure provides the atomic details of its interactions. These structures provide insights into the evolutionary adaptation of the E. histolytica translational machinery and may be explored further for amoebicidal therapeutic intervention. PubMed: 40835601DOI: 10.1038/s41467-025-62767-x PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.1 Å) |
Structure validation
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