8UFM
Crystal Structure of L516C/Y647C Mutant of SARS-Unique Domain (SUD) from SARS-CoV-2
Summary for 8UFM
| Entry DOI | 10.2210/pdb8ufm/pdb |
| Descriptor | Papain-like protease nsp3, FORMIC ACID, ACETATE ION, ... (5 entities in total) |
| Functional Keywords | structural genomics, center for structural genomics of infectious diseases, csgid, sud, sars unique domain, center for structural biology of infectious diseases, csbid, viral protein |
| Biological source | Severe acute respiratory syndrome coronavirus 2 |
| Total number of polymer chains | 1 |
| Total formula weight | 30536.92 |
| Authors | Minasov, G.,Shuvalova, L.,Brunzelle, J.S.,Rosas-Lemus, M.,Kiryukhina, O.,Satchell, K.J.F.,Center for Structural Genomics of Infectious Diseases (CSGID),Center for Structural Biology of Infectious Diseases (CSBID) (deposition date: 2023-10-04, release date: 2023-10-18, Last modification date: 2025-09-24) |
| Primary citation | Rosas-Lemus, M.,Minasov, G.,Brunzelle, J.S.,Taha, T.Y.,Lemak, S.,Yin, S.,Shuvalova, L.,Rosecrans, J.,Khanna, K.,Seifert, H.S.,Savchenko, A.,Stogios, P.J.,Ott, M.,Satchell, K.J.F. Torsional twist of the SARS-CoV and SARS-CoV-2 SUD-N and SUD-M domains. Protein Sci., 34:e70050-e70050, 2025 Cited by PubMed Abstract: Coronavirus non-structural protein 3 (nsp3) forms hexameric crowns of pores in the double membrane vesicle that houses the replication-transcription complex. Nsp3 in SARS-like viruses has three unique domains absent in other coronavirus nsp3 proteins. Two of these, SUD-N (Macrodomain 2) and SUD-M (Macrodomain 3), form two lobes connected by a peptide linker and an interdomain disulfide bridge. We resolve the first complete x-ray structure of SARS-CoV SUD-N/M as well as a mutant variant of SARS-CoV-2 SUD-N/M modified to restore cysteines for interdomain disulfide bond naturally lost by evolution. Comparative analysis of all structures revealed SUD-N and SUD-M are not rigidly associated but rather have significant rotational flexibility. Phylogenetic analysis supports that the potential to form the disulfide bond is common across betacoronavirus isolates from many bat species and civets, but also one or both of the cysteines that form the disulfide bond are absent across isolates from bats and pangolins. The absence of these cysteines does not impact viral replication or protein translation. PubMed: 39969084DOI: 10.1002/pro.70050 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
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