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  The structure of a dimeric form of SARS-CoV-2 polymerase

Jochheim, F. A., Tegunov, D., Hillen, H. S., Schmitzova, J., Kokic, G., Dienemann, C., et al. (2021). The structure of a dimeric form of SARS-CoV-2 polymerase. Communications Biology, 4: 999. doi:10.1038/s42003-021-02529-9.

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 Creators:
Jochheim, F. A.1, Author              
Tegunov, D.1, Author              
Hillen, H. S.2, Author              
Schmitzova, J.1, Author              
Kokic, G.1, Author              
Dienemann, C.1, Author              
Cramer, P.1, Author              
Affiliations:
1Department of Molecular Biology. MPI for Biophysical Chemistry, Max Planck Society, ou_1863498              
2Research Group Structure and Function of Molecular Machines, MPI for Biophysical Chemistry, Max Planck Society, ou_3265856              

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Free keywords: Cryoelectron microscopy; Viral proteins
 Abstract: The coronavirus SARS-CoV-2 uses an RNA-dependent RNA polymerase (RdRp) to replicate and transcribe its genome. Previous structures of the RdRp revealed a monomeric enzyme composed of the catalytic subunit nsp12, two copies of subunit nsp8, and one copy of subunit nsp7. Here we report an alternative, dimeric form of the enzyme and resolve its structure at 5.5 Å resolution. In this structure, the two RdRps contain only one copy of nsp8 each and dimerize via their nsp7 subunits to adopt an antiparallel arrangement. We speculate that the RdRp dimer facilitates template switching during production of sub-genomic RNAs.

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Language(s): eng - English
 Dates: 2021-08-24
 Publication Status: Published online
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 Rev. Type: Peer
 Identifiers: DOI: 10.1038/s42003-021-02529-9
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Title: Communications Biology
Source Genre: Journal
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Pages: 5 Volume / Issue: 4 Sequence Number: 999 Start / End Page: - Identifier: -