7TQL
CryoEM structure of the human 40S small ribosomal subunit in complex with translation initiation factors eIF1A and eIF5B.
Summary for 7TQL
| Entry DOI | 10.2210/pdb7tql/pdb |
| EMDB information | 26067 |
| Descriptor | Eukaryotic translation initiation factor 5B, 40S ribosomal protein S7, 40S ribosomal protein S8, ... (40 entities in total) |
| Functional Keywords | eif5b, translation, initiation, eif1a, ribosome |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 38 |
| Total formula weight | 1234819.23 |
| Authors | Lapointe, C.P.,Grosely, R.,Sokabe, M.,Alvarado, C.,Wang, J.,Montabana, E.,Villa, N.,Shin, B.,Dever, T.,Fraser, C.,Fernandez, I.S.,Puglisi, J.D. (deposition date: 2022-01-26, release date: 2022-04-27, Last modification date: 2024-06-12) |
| Primary citation | Lapointe, C.P.,Grosely, R.,Sokabe, M.,Alvarado, C.,Wang, J.,Montabana, E.,Villa, N.,Shin, B.S.,Dever, T.E.,Fraser, C.S.,Fernandez, I.S.,Puglisi, J.D. eIF5B and eIF1A reorient initiator tRNA to allow ribosomal subunit joining. Nature, 607:185-190, 2022 Cited by PubMed Abstract: Translation initiation defines the identity and quantity of a synthesized protein. The process is dysregulated in many human diseases. A key commitment step is when the ribosomal subunits join at a translation start site on a messenger RNA to form a functional ribosome. Here, we combined single-molecule spectroscopy and structural methods using an in vitro reconstituted system to examine how the human ribosomal subunits join. Single-molecule fluorescence revealed when the universally conserved eukaryotic initiation factors eIF1A and eIF5B associate with and depart from initiation complexes. Guided by single-molecule dynamics, we visualized initiation complexes that contained both eIF1A and eIF5B using single-particle cryo-electron microscopy. The resulting structure revealed how eukaryote-specific contacts between the two proteins remodel the initiation complex to orient the initiator aminoacyl-tRNA in a conformation compatible with ribosomal subunit joining. Collectively, our findings provide a quantitative and architectural framework for the molecular choreography orchestrated by eIF1A and eIF5B during translation initiation in humans. PubMed: 35732735DOI: 10.1038/s41586-022-04858-z PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.2 Å) |
Structure validation
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