7A5H
Structure of the split human mitoribosomal large subunit with rescue factors mtRF-R and MTRES1
This is a non-PDB format compatible entry.
Summary for 7A5H
| Entry DOI | 10.2210/pdb7a5h/pdb |
| EMDB information | 11643 |
| Descriptor | 39S ribosomal protein L2, mitochondrial, 39S ribosomal protein L16, mitochondrial, 39S ribosomal protein L17, mitochondrial, ... (62 entities in total) |
| Functional Keywords | mitochondrial ribosome, ribosome stalling, cryo-em, ribosome |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 59 |
| Total formula weight | 1852055.49 |
| Authors | Desai, N.,Yang, H.,Chandrasekaran, V.,Kazi, R.,Minczuk, M.,Ramakrishnan, V. (deposition date: 2020-08-21, release date: 2020-12-23, Last modification date: 2023-03-01) |
| Primary citation | Desai, N.,Yang, H.,Chandrasekaran, V.,Kazi, R.,Minczuk, M.,Ramakrishnan, V. Elongational stalling activates mitoribosome-associated quality control. Science, 370:1105-1110, 2020 Cited by PubMed Abstract: The human mitochondrial ribosome (mitoribosome) and associated proteins regulate the synthesis of 13 essential subunits of the oxidative phosphorylation complexes. We report the discovery of a mitoribosome-associated quality control pathway that responds to interruptions during elongation, and we present structures at 3.1- to 3.3-angstrom resolution of mitoribosomal large subunits trapped during ribosome rescue. Release factor homolog C12orf65 (mtRF-R) and RNA binding protein C6orf203 (MTRES1) eject the nascent chain and peptidyl transfer RNA (tRNA), respectively, from stalled ribosomes. Recruitment of mitoribosome biogenesis factors to these quality control intermediates suggests additional roles for these factors during mitoribosome rescue. We also report related cryo-electron microscopy structures (3.7 to 4.4 angstrom resolution) of elongating mitoribosomes bound to tRNAs, nascent polypeptides, the guanosine triphosphatase elongation factors mtEF-Tu and mtEF-G1, and the Oxa1L translocase. PubMed: 33243891DOI: 10.1126/science.abc7782 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.3 Å) |
Structure validation
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