6NUS
SARS-Coronavirus NSP12 bound to NSP8 co-factor
Summary for 6NUS
| Entry DOI | 10.2210/pdb6nus/pdb |
| EMDB information | 0520 0521 |
| Descriptor | NSP12, NSP8, ZINC ION (3 entities in total) |
| Functional Keywords | coronavirus, polymerase, non-structural protein, viral protein |
| Biological source | Human SARS coronavirus (SARS-CoV) More |
| Total number of polymer chains | 2 |
| Total formula weight | 131295.84 |
| Authors | Kirchdoerfer, R.N.,Ward, A.B. (deposition date: 2019-02-01, release date: 2019-05-29, Last modification date: 2024-03-20) |
| Primary citation | Kirchdoerfer, R.N.,Ward, A.B. Structure of the SARS-CoV nsp12 polymerase bound to nsp7 and nsp8 co-factors. Nat Commun, 10:2342-2342, 2019 Cited by PubMed Abstract: Recent history is punctuated by the emergence of highly pathogenic coronaviruses such as SARS- and MERS-CoV into human circulation. Upon infecting host cells, coronaviruses assemble a multi-subunit RNA-synthesis complex of viral non-structural proteins (nsp) responsible for the replication and transcription of the viral genome. Here, we present the 3.1 Å resolution structure of the SARS-CoV nsp12 polymerase bound to its essential co-factors, nsp7 and nsp8, using single particle cryo-electron microscopy. nsp12 possesses an architecture common to all viral polymerases as well as a large N-terminal extension containing a kinase-like fold and is bound by two nsp8 co-factors. This structure illuminates the assembly of the coronavirus core RNA-synthesis machinery, provides key insights into nsp12 polymerase catalysis and fidelity and acts as a template for the design of novel antiviral therapeutics. PubMed: 31138817DOI: 10.1038/s41467-019-10280-3 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.5 Å) |
Structure validation
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