6ZOK
SARS-CoV-2-Nsp1-40S complex, focused on body
Summary for 6ZOK
| Entry DOI | 10.2210/pdb6zok/pdb |
| EMDB information | 11321 |
| Descriptor | 18S ribosomal RNA, 40S ribosomal protein S11, 40S ribosomal protein S13, ... (24 entities in total) |
| Functional Keywords | inhibitor, mrna channel, 40s ribosomal subunit, translation |
| Biological source | Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) More |
| Total number of polymer chains | 22 |
| Total formula weight | 1000221.22 |
| Authors | Schubert, K.,Karousis, E.D.,Jomaa, A.,Scaiola, A.,Echeverria, B.,Gurzeler, L.-A.,Leibundgut, M.,Thiel, V.,Muehlemann, O.,Ban, N. (deposition date: 2020-07-07, release date: 2020-07-29, Last modification date: 2021-02-10) |
| Primary citation | Schubert, K.,Karousis, E.D.,Jomaa, A.,Scaiola, A.,Echeverria, B.,Gurzeler, L.A.,Leibundgut, M.,Thiel, V.,Muhlemann, O.,Ban, N. SARS-CoV-2 Nsp1 binds the ribosomal mRNA channel to inhibit translation. Nat.Struct.Mol.Biol., 27:959-966, 2020 Cited by PubMed Abstract: The SARS-CoV-2 non-structural protein 1 (Nsp1), also referred to as the host shutoff factor, suppresses host innate immune functions. By combining cryo-electron microscopy and biochemistry, we show that SARS-CoV-2 Nsp1 binds to the human 40S subunit in ribosomal complexes, including the 43S pre-initiation complex and the non-translating 80S ribosome. The protein inserts its C-terminal domain into the mRNA channel, where it interferes with mRNA binding. We observe translation inhibition in the presence of Nsp1 in an in vitro translation system and in human cells. Based on the high-resolution structure of the 40S-Nsp1 complex, we identify residues of Nsp1 crucial for mediating translation inhibition. We further show that the full-length 5' untranslated region of the genomic viral mRNA stimulates translation in vitro, suggesting that SARS-CoV-2 combines global inhibition of translation by Nsp1 with efficient translation of the viral mRNA to allow expression of viral genes. PubMed: 32908316DOI: 10.1038/s41594-020-0511-8 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.8 Å) |
Structure validation
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