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

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.

SUBMITTER: Jochheim FA

PROVIDER: S-EPMC8385044 | biostudies-literature | 2021 Aug

REPOSITORIES: biostudies-literature

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

Jochheim Florian A FA Tegunov Dimitry D Hillen Hauke S HS Schmitzová Jana J Kokic Goran G Dienemann Christian C Cramer Patrick P

Communications biology 20210824 1

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 antipara ...[more]

PMID: 34429502

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