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9FIA

SSU(body) structure derived from the SSU sample of the mitoribosome from T. gondii.

This is a non-PDB format compatible entry.
Summary for 9FIA
Entry DOI10.2210/pdb9fia/pdb
EMDB information50470
DescriptorMitochondrial ribosomal protein, mS145, DnaJ domain-containing protein, Mitochondrial ribosomal protein, mS137, ... (66 entities in total)
Functional Keywordscomplex, translation, rrna, ribosome
Biological sourceToxoplasma gondii
More
Total number of polymer chains69
Total formula weight2007938.51
Authors
Rocha, R.E.O.,Barua, S.,Boissier, F.,Nguyen, T.T.,Hashem, Y. (deposition date: 2024-05-28, release date: 2024-12-11, Last modification date: 2025-01-01)
Primary citationWang, C.,Kassem, S.,Rocha, R.E.O.,Sun, P.,Nguyen, T.T.,Kloehn, J.,Liu, X.,Brusini, L.,Bonavoglia, A.,Barua, S.,Boissier, F.,Lucia Del Cistia, M.,Peng, H.,Tang, X.,Xie, F.,Wang, Z.,Vadas, O.,Suo, X.,Hashem, Y.,Soldati-Favre, D.,Jia, Y.
Apicomplexan mitoribosome from highly fragmented rRNAs to a functional machine.
Nat Commun, 15:10689-10689, 2024
Cited by
PubMed Abstract: The phylum Apicomplexa comprises eukaryotic parasites that cause fatal diseases affecting millions of people and animals worldwide. Their mitochondrial genomes have been significantly reduced, leaving only three protein-coding genes and highly fragmented mitoribosomal rRNAs, raising challenging questions about mitoribosome composition, assembly and structure. Our study reveals how Toxoplasma gondii assembles over 40 mt-rRNA fragments using exclusively nuclear-encoded mitoribosomal proteins and three lineage-specific families of RNA-binding proteins. Among these are four proteins from the Apetala2/Ethylene Response Factor (AP2/ERF) family, originally known as transcription factors in plants and Apicomplexa, now repurposed as essential mitoribosome components. Cryo-EM analysis of the mitoribosome structure demonstrates how these AP2 proteins function as RNA binders to maintain mitoribosome integrity. The mitoribosome is also decorated with members of lineage-specific RNA-binding proteins belonging to RAP (RNA-binding domain abundant in Apicomplexa) proteins and HPR (heptatricopeptide repeat) families, highlighting the unique adaptations of these parasites. Solving the molecular puzzle of apicomplexan mitoribosome could inform the development of therapeutic strategies targeting organellar translation.
PubMed: 39690155
DOI: 10.1038/s41467-024-55033-z
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.29 Å)
Structure validation

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