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

Florian A JochheimDimitry TegunovHauke S HillenJana SchmitzováGoran KokicChristian DienemannPatrick Cramer
Published in: Communications biology (2021)
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.
Keyphrases
  • sars cov
  • respiratory syndrome coronavirus
  • protein kinase
  • gene expression
  • genome wide
  • copy number