8EKE
Cryo-EM structure of SARS CoV-2 Mpro WT protease
Summary for 8EKE
| Entry DOI | 10.2210/pdb8eke/pdb |
| EMDB information | 28200 |
| Descriptor | 3C-like proteinase nsp5 (1 entity in total) |
| Functional Keywords | main protease, mpro, sars cov-2, polyprotein, viral protein |
| Biological source | Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2, 2019-nCoV, COVID-19 virus) |
| Total number of polymer chains | 2 |
| Total formula weight | 67586.96 |
| Authors | Narwal, M.,Edwards, T.,Armache, J.P.,Murakami, K.S. (deposition date: 2022-09-20, release date: 2023-04-26, Last modification date: 2024-06-19) |
| Primary citation | Narwal, M.,Armache, J.P.,Edwards, T.J.,Murakami, K.S. SARS-CoV-2 polyprotein substrate regulates the stepwise M pro cleavage reaction. J.Biol.Chem., 299:104697-104697, 2023 Cited by PubMed Abstract: The processing of the Coronavirus polyproteins pp1a and pp1ab by the main protease M to produce mature proteins is a crucial event in virus replication and a promising target for antiviral drug development. M cleaves polyproteins in a defined order, but how M and/or the polyproteins determine the order of cleavage remains enigmatic due to a lack of structural information about polyprotein-bound M. Here, we present the cryo-EM structures of SARS-CoV-2 M in an apo form and in complex with the nsp7-10 region of the pp1a polyprotein. The complex structure shows that M interacts with only the recognition site residues between nsp9 and nsp10, without any association with the rest of the polyprotein. Comparison between the apo form and polyprotein-bound structures of M highlights the flexible nature of the active site region of M, which allows it to accommodate ten recognition sites found in the polyprotein. These observations suggest that the role of M in selecting a preferred cleavage site is limited and underscores the roles of the structure, conformation, and/or dynamics of the polyproteins in determining the sequence of polyprotein cleavage by M. PubMed: 37044215DOI: 10.1016/j.jbc.2023.104697 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.36 Å) |
Structure validation
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