7L20
Cryo-EM structure of the human 39S mitoribosomal subunit in complex with RRFmt and EF-G2mt.
This is a non-PDB format compatible entry.
Summary for 7L20
| Entry DOI | 10.2210/pdb7l20/pdb |
| EMDB information | 23121 |
| Descriptor | 16S rRNA mitochondrial, 39S ribosomal protein L20, mitochondrial, 39S ribosomal protein L21, mitochondrial, ... (59 entities in total) |
| Functional Keywords | cryo-em, mammalian, mito-ribosome, mtefg2, mtrrf, ribosome |
| Biological source | Homo sapiens More |
| Total number of polymer chains | 58 |
| Total formula weight | 1906439.05 |
| Authors | Agrawal, E.,Koripella, R. (deposition date: 2020-12-15, release date: 2021-05-12, Last modification date: 2024-11-20) |
| Primary citation | Koripella, R.K.,Deep, A.,Agrawal, E.K.,Keshavan, P.,Banavali, N.K.,Agrawal, R.K. Distinct mechanisms of the human mitoribosome recycling and antibiotic resistance. Nat Commun, 12:3607-3607, 2021 Cited by PubMed Abstract: Ribosomes are recycled for a new round of translation initiation by dissociation of ribosomal subunits, messenger RNA and transfer RNA from their translational post-termination complex. Here we present cryo-EM structures of the human 55S mitochondrial ribosome (mitoribosome) and the mitoribosomal large 39S subunit in complex with mitoribosome recycling factor (RRF) and a recycling-specific homolog of elongation factor G (EF-G2). These structures clarify an unusual role of a mitochondria-specific segment of RRF, identify the structural distinctions that confer functional specificity to EF-G2, and show that the deacylated tRNA remains with the dissociated 39S subunit, suggesting a distinct sequence of events in mitoribosome recycling. Furthermore, biochemical and structural analyses reveal that the molecular mechanism of antibiotic fusidic acid resistance for EF-G2 is markedly different from that of mitochondrial elongation factor EF-G1, suggesting that the two human EF-Gs have evolved diversely to negate the effect of a bacterial antibiotic. PubMed: 34127662DOI: 10.1038/s41467-021-23726-4 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.15 Å) |
Structure validation
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