8CSP
Human mitochondrial small subunit assembly intermediate (State A)
Summary for 8CSP
| Entry DOI | 10.2210/pdb8csp/pdb |
| EMDB information | 26966 |
| Descriptor | 28S ribosomal protein S34, mitochondrial, 28S ribosomal protein S24, mitochondrial, 28S ribosomal protein S5, mitochondrial, ... (41 entities in total) |
| Functional Keywords | ribonucleoprotein complex, mitochondria biogenesis, ribosome |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 33 |
| Total formula weight | 1348949.02 |
| Authors | Harper, N.J.,Burnside, C.,Klinge, S. (deposition date: 2022-05-13, release date: 2022-12-14, Last modification date: 2024-06-12) |
| Primary citation | Harper, N.J.,Burnside, C.,Klinge, S. Principles of mitoribosomal small subunit assembly in eukaryotes. Nature, 614:175-181, 2023 Cited by PubMed Abstract: Mitochondrial ribosomes (mitoribosomes) synthesize proteins encoded within the mitochondrial genome that are assembled into oxidative phosphorylation complexes. Thus, mitoribosome biogenesis is essential for ATP production and cellular metabolism. Here we used cryo-electron microscopy to determine nine structures of native yeast and human mitoribosomal small subunit assembly intermediates, illuminating the mechanistic basis for how GTPases are used to control early steps of decoding centre formation, how initial rRNA folding and processing events are mediated, and how mitoribosomal proteins have active roles during assembly. Furthermore, this series of intermediates from two species with divergent mitoribosomal architecture uncovers both conserved principles and species-specific adaptations that govern the maturation of mitoribosomal small subunits in eukaryotes. By revealing the dynamic interplay between assembly factors, mitoribosomal proteins and rRNA that are required to generate functional subunits, our structural analysis provides a vignette for how molecular complexity and diversity can evolve in large ribonucleoprotein assemblies. PubMed: 36482135DOI: 10.1038/s41586-022-05621-0 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.66 Å) |
Structure validation
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