7AM2
Intermediate assembly of the Large subunit from Leishmania major mitochondrial ribosome
This is a non-PDB format compatible entry.
Summary for 7AM2
| Entry DOI | 10.2210/pdb7am2/pdb |
| EMDB information | 11821 |
| Descriptor | Ribosomal protein L3-like protein, bL21m, uL22m, ... (79 entities in total) |
| Functional Keywords | ribosome, mitochondria, kinetoplastid |
| Biological source | Leishmania tarentolae More |
| Total number of polymer chains | 78 |
| Total formula weight | 8589490.22 |
| Authors | Soufari, H.,Waltz, F.,Parrot, C.,Bochler, A.,Hashem, Y. (deposition date: 2020-10-07, release date: 2021-04-28, Last modification date: 2024-10-09) |
| Primary citation | Soufari, H.,Waltz, F.,Parrot, C.,Durrieu-Gaillard, S.,Bochler, A.,Kuhn, L.,Sissler, M.,Hashem, Y. Structure of the mature kinetoplastids mitoribosome and insights into its large subunit biogenesis. Proc.Natl.Acad.Sci.USA, 117:29851-29861, 2020 Cited by PubMed Abstract: Kinetoplastids are unicellular eukaryotic parasites responsible for such human pathologies as Chagas disease, sleeping sickness, and leishmaniasis. They have a single large mitochondrion, essential for the parasite survival. In kinetoplastid mitochondria, most of the molecular machineries and gene expression processes have significantly diverged and specialized, with an extreme example being their mitochondrial ribosomes. These large complexes are in charge of translating the few essential mRNAs encoded by mitochondrial genomes. Structural studies performed in already highlighted the numerous peculiarities of these mitoribosomes and the maturation of their small subunit. However, several important aspects mainly related to the large subunit (LSU) remain elusive, such as the structure and maturation of its ribosomal RNA. Here we present a cryo-electron microscopy study of the protozoans and mitoribosomes. For both species, we obtained the structure of their mature mitoribosomes, complete rRNA of the LSU, as well as previously unidentified ribosomal proteins. In addition, we introduce the structure of an LSU assembly intermediate in the presence of 16 identified maturation factors. These maturation factors act on both the intersubunit and the solvent sides of the LSU, where they refold and chemically modify the rRNA and prevent early translation before full maturation of the LSU. PubMed: 33168716DOI: 10.1073/pnas.2011301117 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.4 Å) |
Structure validation
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