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| Title | Structure of the SARS-CoV nsp12 polymerase bound to nsp7 and nsp8 co-factors. |
|---|---|
| Journal, issue, pages | Nat Commun, Vol. 10, Issue 1, Page 2342, Year 2019 |
| Publish date | May 28, 2019 |
 Authors | Robert N Kirchdoerfer / Andrew B Ward /  |
| 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 ...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. |
 External links | Nat Commun / PubMed:31138817 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 3.1 - 3.5 Å |
| Structure data | |
| Chemicals |  ChemComp-ZN: |
| Source |
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 Keywords |  VIRAL PROTEIN / coronavirus / polymerase / non-structural protein |
