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8D8J

Yeast mitochondrial small subunit assembly intermediate (State 1)

Summary for 8D8J
Entry DOI10.2210/pdb8d8j/pdb
EMDB information27249
DescriptorProbable S-adenosyl-L-methionine-dependent RNA methyltransferase RSM22, mitochondrial, 37S ribosomal protein NAM9, mitochondrial, 37S ribosomal protein S5, mitochondrial, ... (18 entities in total)
Functional Keywordsribonucleoprotein complex mitochondria biogenesis, ribosome
Biological sourceSaccharomyces cerevisiae (baker's yeast)
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Total number of polymer chains16
Total formula weight1085445.55
Authors
Burnside, C.,Harper, N.,Klinge, S. (deposition date: 2022-06-08, release date: 2022-12-21, Last modification date: 2024-06-12)
Primary citationHarper, 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: 36482135
DOI: 10.1038/s41586-022-05621-0
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.8 Å)
Structure validation

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