9YGM
Babesia divergens ribosome structure by single-particle cryo-EM (3D class3, E-site tRNA)
This is a non-PDB format compatible entry.
Summary for 9YGM
| Entry DOI | 10.2210/pdb9ygm/pdb |
| EMDB information | 72933 |
| Descriptor | 5S ribosomal RNA, 60S ribosomal protein eL18, 60S ribosomal protein uL22, ... (84 entities in total) |
| Functional Keywords | trnas, rna modification, 80s, ribosome |
| Biological source | Babesia divergens More |
| Total number of polymer chains | 80 |
| Total formula weight | 3137070.15 |
| Authors | Gutierrez-Vargas, C.,Izhaki-Tavor, L.S.,Leger-Abraham, M. (deposition date: 2025-09-29, release date: 2026-06-24, Last modification date: 2026-07-01) |
| Primary citation | Gutierrez-Vargas, C.,Izhaki-Tavor, L.S.,Calvopina-Chavez, D.,Keroack, C.D.,Copello, P.,Duraisingh, M.T.,Leger-Abraham, M. Ribosomal Architecture and rRNA Modification Landscape in the Tick-Borne Parasite Babesia divergens. Biorxiv, 2025 Cited by PubMed Abstract: is a tick-borne intracellular apicomplexan parasite responsible for diseases ranging from mild to fatal, with a broadening geographic distribution. Due to the complex life cycle of species, their survival depends on the precise control of gene expression, which is primarily regulated by epigenetic, transcriptional, and post-transcriptional mechanisms. High-resolution structural information on key components of the translation machinery, such as ribosomes, could aid in the development of antiparasitic drugs. Here, we report cryo-EM ribosome structures (2.6 Å) from the tick-borne apicomplexan pathogen , showing associated tRNAs, an mRNA fragment, and RACK1, a signaling scaffold crucial to translation regulation. Density map analysis displays ribosome regions at atomic resolution (1.7 Å), which, when combined with nanopore sequencing, enabled the comprehensive identification of rRNA modifications, including modifications unreported in other organisms. The new rRNA modifications localize not only to the reduced rRNA expansion segments but also to functionally essential ribosomal sites, uncovering new avenues for therapeutic intervention against babesiosis. PubMed: 41293005DOI: 10.1101/2025.11.11.687446 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.7 Å) |
Structure validation
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