7UU9
Crystal structure of the SARS-CoV-2 main protease in its apo-form
Summary for 7UU9
| Entry DOI | 10.2210/pdb7uu9/pdb |
| Descriptor | 3C-like proteinase nsp5 (2 entities in total) |
| Functional Keywords | main protease, viral protein, hydrolase |
| Biological source | Severe acute respiratory syndrome coronavirus 2 |
| Total number of polymer chains | 1 |
| Total formula weight | 33873.55 |
| Authors | Yang, K.S.,Liu, W.R. (deposition date: 2022-04-28, release date: 2023-01-25, Last modification date: 2024-10-09) |
| Primary citation | Yang, K.S.,Blankenship, L.R.,Kuo, S.A.,Sheng, Y.J.,Li, P.,Fierke, C.A.,Russell, D.H.,Yan, X.,Xu, S.,Liu, W.R. A Novel Y-Shaped, S-O-N-O-S-Bridged Cross-Link between Three Residues C22, C44, and K61 Is Frequently Observed in the SARS-CoV-2 Main Protease. Acs Chem.Biol., 18:449-455, 2023 Cited by PubMed Abstract: As the COVID-19 pathogen, SARS-CoV-2 relies on its main protease (M) for pathogenesis and replication. During crystallographic analyses of M crystals that were exposed to the air, a uniquely Y-shaped, S-O-N-O-S-bridged post-translational cross-link that connects three residues C22, C44, and K61 at their side chains was frequently observed. As a novel covalent modification, this cross-link serves potentially as a redox switch to regulate the catalytic activity of M, a demonstrated drug target of COVID-19. The formation of this linkage leads to a much more open active site that can potentially be targeted for the development of novel SARS-CoV-2 antivirals. The structural rearrangement of M by this cross-link indicates that small molecules that lock M in the cross-linked form can potentially be used with other active-site-targeting molecules such as paxlovid for synergistic effects in inhibiting SARS-CoV-2 viral replication. PubMed: 36629751DOI: 10.1021/acschembio.2c00695 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.47 Å) |
Structure validation
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