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TitleThe structure of a dimeric form of SARS-CoV-2 polymerase.
Journal, issue, pagesCommun Biol, Vol. 4, Issue 1, Page 999, Year 2021
Publish dateAug 24, 2021
AuthorsFlorian A Jochheim / Dimitry Tegunov / Hauke S Hillen / Jana Schmitzová / Goran Kokic / Christian Dienemann / Patrick Cramer /
PubMed AbstractThe 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 ...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.
External linksCommun Biol / PubMed:34429502 / PubMed Central
MethodsEM (single particle)
Resolution5.5 Å
Structure data

13116

7oyg

EMDB-13116, PDB-7oyg:
Dimeric form of SARS-CoV-2 RNA-dependent RNA polymerase
Method: EM (single particle) / Resolution: 5.5 Å

Chemicals

ChemComp-ZN:
Unknown entry

Source
  • severe acute respiratory syndrome coronavirus 2
KeywordsVIRAL PROTEIN / SARS-CoV-2 / Polymerase / Transcription / Replication / RNA / Dimer

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