6RW5
Structure of human mitochondrial 28S ribosome in complex with mitochondrial IF2 and IF3
This is a non-PDB format compatible entry.
Summary for 6RW5
| Entry DOI | 10.2210/pdb6rw5/pdb |
| EMDB information | 10022 |
| Descriptor | 12S mitochondrial rRNA, 28S ribosomal protein S12, mitochondrial, 28S ribosomal protein S14, mitochondrial, ... (43 entities in total) |
| Functional Keywords | ribosomal small subunit, initiation complex, initiation factor, ribosome |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 33 |
| Total formula weight | 1258060.63 |
| Authors | Itoh, Y.,Khawaja, A.,Rorbach, J.,Amunts, A. (deposition date: 2019-06-03, release date: 2020-06-03, Last modification date: 2024-04-24) |
| Primary citation | Khawaja, A.,Itoh, Y.,Remes, C.,Spahr, H.,Yukhnovets, O.,Hofig, H.,Amunts, A.,Rorbach, J. Distinct pre-initiation steps in human mitochondrial translation. Nat Commun, 11:2932-2932, 2020 Cited by PubMed Abstract: Translation initiation in human mitochondria relies upon specialized mitoribosomes and initiation factors, mtIF2 and mtIF3, which have diverged from their bacterial counterparts. Here we report two distinct mitochondrial pre-initiation assembly steps involving those factors. Single-particle cryo-EM revealed that in the first step, interactions between mitochondria-specific protein mS37 and mtIF3 keep the small mitoribosomal subunit in a conformation favorable for a subsequent accommodation of mtIF2 in the second step. Combination with fluorescence cross-correlation spectroscopy analyses suggests that mtIF3 promotes complex assembly without mRNA or initiator tRNA binding, where exclusion is achieved by the N-terminal and C-terminal domains of mtIF3. Finally, the association of large mitoribosomal subunit is required for initiator tRNA and leaderless mRNA recruitment to form a stable initiation complex. These data reveal fundamental aspects of mammalian protein synthesis that are specific to mitochondria. PubMed: 32522994DOI: 10.1038/s41467-020-16503-2 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.14 Å) |
Structure validation
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