6YBD
Structure of a human 48S translational initiation complex - eIF3
Summary for 6YBD
Entry DOI | 10.2210/pdb6ybd/pdb |
EMDB information | 10769 |
Descriptor | Eukaryotic translation initiation factor 3 subunit M, 40S ribosomal protein S17, 40S ribosomal protein S2, ... (19 entities in total) |
Functional Keywords | eif3, ribosome, translation, initiation complex |
Biological source | Homo sapiens (Human) More |
Total number of polymer chains | 19 |
Total formula weight | 797990.08 |
Authors | Brito Querido, J.,Sokabe, M.,Kraatz, S.,Gordiyenko, Y.,Skehel, M.,Fraser, C.,Ramakrishnan, V. (deposition date: 2020-03-16, release date: 2020-09-16, Last modification date: 2024-05-22) |
Primary citation | Brito Querido, J.,Sokabe, M.,Kraatz, S.,Gordiyenko, Y.,Skehel, J.M.,Fraser, C.S.,Ramakrishnan, V. Structure of a human 48Stranslational initiation complex. Science, 369:1220-1227, 2020 Cited by PubMed Abstract: A key step in translational initiation is the recruitment of the 43 preinitiation complex by the cap-binding complex [eukaryotic initiation factor 4F (eIF4F)] at the 5' end of messenger RNA (mRNA) to form the 48 initiation complex (i.e., the 48). The 48 then scans along the mRNA to locate a start codon. To understand the mechanisms involved, we used cryo-electron microscopy to determine the structure of a reconstituted human 48 The structure reveals insights into early events of translation initiation complex assembly, as well as how eIF4F interacts with subunits of eIF3 near the mRNA exit channel in the 43 The location of eIF4F is consistent with a slotting model of mRNA recruitment and suggests that downstream mRNA is unwound at least in part by being "pulled" through the 40 subunit during scanning. PubMed: 32883864DOI: 10.1126/science.aba4904 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.3 Å) |
Structure validation
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