Summary for 7ZJX
| Entry DOI | 10.2210/pdb7zjx/pdb |
| EMDB information | 14752 |
| Descriptor | Selenocysteine insertion sequence-binding protein 2, 60S ribosomal protein L6, 60S ribosomal Protein uL30, ... (84 entities in total) |
| Functional Keywords | selenocysteine, recoding, 80s, ribosome |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 83 |
| Total formula weight | 4195451.53 |
| Authors | Hilal, T.,Simonovic, M.,Spahn, C.M.T. (deposition date: 2022-04-12, release date: 2022-09-07, Last modification date: 2025-10-01) |
| Primary citation | Hilal, T.,Killam, B.Y.,Grozdanovic, M.,Dobosz-Bartoszek, M.,Loerke, J.,Burger, J.,Mielke, T.,Copeland, P.R.,Simonovic, M.,Spahn, C.M.T. Structure of the mammalian ribosome as it decodes the selenocysteine UGA codon. Science, 376:1338-1343, 2022 Cited by PubMed Abstract: The elongation of eukaryotic selenoproteins relies on a poorly understood process of interpreting in-frame UGA stop codons as selenocysteine (Sec). We used cryo-electron microscopy to visualize Sec UGA recoding in mammals. A complex between the noncoding Sec-insertion sequence (SECIS), SECIS-binding protein 2 (SBP2), and 40 ribosomal subunit enables Sec-specific elongation factor eEFSec to deliver Sec. eEFSec and SBP2 do not interact directly but rather deploy their carboxyl-terminal domains to engage with the opposite ends of the SECIS. By using its Lys-rich and carboxyl-terminal segments, the ribosomal protein eS31 simultaneously interacts with Sec-specific transfer RNA (tRNA) and SBP2, which further stabilizes the assembly. eEFSec is indiscriminate toward l-serine and facilitates its misincorporation at Sec UGA codons. Our results support a fundamentally distinct mechanism of Sec UGA recoding in eukaryotes from that in bacteria. PubMed: 35709277DOI: 10.1126/science.abg3875 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.1 Å) |
Structure validation
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