Summary for 7N6N
| Entry DOI | 10.2210/pdb7n6n/pdb |
| Descriptor | 3C-like proteinase (2 entities in total) |
| Functional Keywords | mpro, main protease, covid-19, sars-cov-2, 3cl, hydrolase |
| Biological source | Severe acute respiratory syndrome coronavirus 2 (2019-nCoV, SARS-CoV-2) More |
| Total number of polymer chains | 3 |
| Total formula weight | 69910.66 |
| Authors | Noske, G.D.,Nakamura, A.M.,Gawriljuk, V.O.,Lima, G.M.A.,Zeri, A.C.M.,Nascimento, A.F.Z.,Fernandes, R.S.,Oliva, G.,Godoy, A.S. (deposition date: 2021-06-08, release date: 2021-06-16, Last modification date: 2023-10-18) |
| Primary citation | Noske, G.D.,Nakamura, A.M.,Gawriljuk, V.O.,Fernandes, R.S.,Lima, G.M.A.,Rosa, H.V.D.,Pereira, H.D.,Zeri, A.C.M.,Nascimento, A.F.Z.,Freire, M.C.L.C.,Fearon, D.,Douangamath, A.,von Delft, F.,Oliva, G.,Godoy, A.S. A Crystallographic Snapshot of SARS-CoV-2 Main Protease Maturation Process. J.Mol.Biol., 433:167118-167118, 2021 Cited by PubMed Abstract: SARS-CoV-2 is the causative agent of COVID-19. The dimeric form of the viral M is responsible for the cleavage of the viral polyprotein in 11 sites, including its own N and C-terminus. The lack of structural information for intermediary forms of M is a setback for the understanding its self-maturation process. Herein, we used X-ray crystallography combined with biochemical data to characterize multiple forms of SARS-CoV-2 M. For the immature form, we show that extra N-terminal residues caused conformational changes in the positioning of domain-three over the active site, hampering the dimerization and diminishing its activity. We propose that this form preludes the cis and trans-cleavage of N-terminal residues. Using fragment screening, we probe new cavities in this form which can be used to guide therapeutic development. Furthermore, we characterized a serine site-directed mutant of the M bound to its endogenous N and C-terminal residues during dimeric association stage of the maturation process. We suggest this form is a transitional state during the C-terminal trans-cleavage. This data sheds light in the structural modifications of the SARS-CoV-2 main protease during its self-maturation process. PubMed: 34174328DOI: 10.1016/j.jmb.2021.167118 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
Download full validation report
