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Structure of the SARS-CoV nsp12 polymerase bound to nsp7 and nsp8 co-factors
Open accessAbstract
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.
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Isolation and characterization of a bat SARS-like coronavirus that uses the ACE2 receptor
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Structural basis for inhibition of the RNA-dependent RNA polymerase from SARS-CoV-2 by remdesivir
Yin, W., Mao, C., Luan, X., Shen, D.-D., Shen, Q., Su, H., Wang, X., Zhou, F., Zhao, W., Gao, M., et al. (2020) · Science · doi:10.1126/science.abc1560 · Cited by 1,219
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A molecular pore spans the double membrane of the coronavirus replication organelle
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COVID-19: Drug Targets and Potential Treatments
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Metadata
- Authors
- Kirchdoerfer, R. N., & Ward, A. B.
- Venue
- Nature Communications
- Published
- 2019-05-28
- Volume
- 10
- Issue
- 1
- Pages
- 2342-2342
- ISSN
- 2041-1723 (ISSN-L)
- OpenAlex
- W2914796231
- Cited by
- 896
- References
- 3
- FWCI
- 114.11
- Type
- journal article
- Language
- en
- Open access
- gold
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