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5OOL

Structure of a native assembly intermediate of the human mitochondrial ribosome with unfolded interfacial rRNA

Summary for 5OOL
Entry DOI10.2210/pdb5ool/pdb
EMDB information3842
Descriptor16S ribosomal RNA, 39S ribosomal protein L14, mitochondrial, 39S ribosomal protein L15, mitochondrial, ... (59 entities in total)
Functional Keywordsribosome, mitochondria, biogenesis, translation, electron cryomicroscopy
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains56
Total formula weight1797380.72
Authors
Brown, A.,Rathore, S.,Kimanius, D.,Aibara, S.,Bai, X.C.,Rorbach, J.,Amunts, A.,Ramakrishnan, V. (deposition date: 2017-08-08, release date: 2017-09-13, Last modification date: 2025-04-09)
Primary citationBrown, A.,Rathore, S.,Kimanius, D.,Aibara, S.,Bai, X.C.,Rorbach, J.,Amunts, A.,Ramakrishnan, V.
Structures of the human mitochondrial ribosome in native states of assembly.
Nat. Struct. Mol. Biol., 24:866-869, 2017
Cited by
PubMed Abstract: Mammalian mitochondrial ribosomes (mitoribosomes) have less rRNA content and 36 additional proteins compared with the evolutionarily related bacterial ribosome. These differences make the assembly of mitoribosomes more complex than the assembly of bacterial ribosomes, but the molecular details of mitoribosomal biogenesis remain elusive. Here, we report the structures of two late-stage assembly intermediates of the human mitoribosomal large subunit (mt-LSU) isolated from a native pool within a human cell line and solved by cryo-EM to ∼3-Å resolution. Comparison of the structures reveals insights into the timing of rRNA folding and protein incorporation during the final steps of ribosomal maturation and the evolutionary adaptations that are required to preserve biogenesis after the structural diversification of mitoribosomes. Furthermore, the structures redefine the ribosome silencing factor (RsfS) family as multifunctional biogenesis factors and identify two new assembly factors (L0R8F8 and mt-ACP) not previously implicated in mitoribosomal biogenesis.
PubMed: 28892042
DOI: 10.1038/nsmb.3464
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.06 Å)
Structure validation

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