Structure of the SARS-CoV nsp12 polymerase bound to nsp7 and nsp8 co-factors

Robert N. Kirchdoerfer () and Andrew B. Ward
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Robert N. Kirchdoerfer: The Scripps Research Institute
Andrew B. Ward: The Scripps Research Institute

Nature Communications, 2019, vol. 10, issue 1, 1-9

Abstract: 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.

Date: 2019
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DOI: 10.1038/s41467-019-10280-3

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