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TitleStructural Basis for Helicase-Polymerase Coupling in the SARS-CoV-2 Replication-Transcription Complex.
Journal, issue, pagesCell, Vol. 182, Issue 6, Page 1560-1573.e13, Year 2020
Publish dateSep 17, 2020
AuthorsJames Chen / Brandon Malone / Eliza Llewellyn / Michael Grasso / Patrick M M Shelton / Paul Dominic B Olinares / Kashyap Maruthi / Edward T Eng / Hasan Vatandaslar / Brian T Chait / Tarun M Kapoor / Seth A Darst / Elizabeth A Campbell /
PubMed AbstractSARS-CoV-2 is the causative agent of the 2019-2020 pandemic. The SARS-CoV-2 genome is replicated and transcribed by the RNA-dependent RNA polymerase holoenzyme (subunits nsp7/nsp8/nsp12) along with a ...SARS-CoV-2 is the causative agent of the 2019-2020 pandemic. The SARS-CoV-2 genome is replicated and transcribed by the RNA-dependent RNA polymerase holoenzyme (subunits nsp7/nsp8/nsp12) along with a cast of accessory factors. One of these factors is the nsp13 helicase. Both the holo-RdRp and nsp13 are essential for viral replication and are targets for treating the disease COVID-19. Here we present cryoelectron microscopic structures of the SARS-CoV-2 holo-RdRp with an RNA template product in complex with two molecules of the nsp13 helicase. The Nidovirales order-specific N-terminal domains of each nsp13 interact with the N-terminal extension of each copy of nsp8. One nsp13 also contacts the nsp12 thumb. The structure places the nucleic acid-binding ATPase domains of the helicase directly in front of the replicating-transcribing holo-RdRp, constraining models for nsp13 function. We also observe ADP-Mg bound in the nsp12 N-terminal nidovirus RdRp-associated nucleotidyltransferase domain, detailing a new pocket for anti-viral therapy development.
External linksCell / PubMed:32783916 / PubMed Central
MethodsEM (single particle)
Resolution3.5 - 3.6 Å
Structure data

22160

6xez

EMDB-22160, PDB-6xez:
Structure of SARS-CoV-2 replication-transcription complex bound to nsp13 helicase - nsp13(2)-RTC
Method: EM (single particle) / Resolution: 3.5 Å

EMDB-49420: SARS-CoV-2 nsp13(2)-RTC (no detergent)
Method: EM (single particle) / Resolution: 3.6 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-MG:
Unknown entry

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

ChemComp-1N7:
CHAPSO / detergent*YM

ChemComp-AF3:
ALUMINUM FLUORIDE

Source
  • severe acute respiratory syndrome coronavirus 2
KeywordsTRANSFERASE/HYDROLASE/RNA / RNA-dependent RNA polymerase / viral replication-transcription complex / transcription / viral proteins / TRANSFERASE-HYDROLASE-RNA complex

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