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TitleStructural basis for helicase-polymerase coupling in the SARS-CoV-2 replication-transcription complex.
Journal, issue, pagesbioRxiv, Year 2020
Publish dateJul 13, 2020
AuthorsJames Chen / Brandon Malone / Eliza Llewellyn / Michael Grasso / Patrick M M Shelton / Paul Dominic B Olinares / Kashyap Maruthi / Ed Eng / Hasan Vatandaslar / Brian T Chait / Tarun 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-transcribed by the RNA-dependent RNA polymerase holoenzyme (subunits nsp7/nsp82/nsp12) along with a ...SARS-CoV-2 is the causative agent of the 2019-2020 pandemic. The SARS-CoV-2 genome is replicated-transcribed by the RNA-dependent RNA polymerase holoenzyme (subunits nsp7/nsp82/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 cryo-electron microscopic structures of the SARS-CoV-2 holo-RdRp with an RNA template-product in complex with two molecules of the nsp13 helicase. The Nidovirus-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-Mg2+ bound in the nsp12 N-terminal nidovirus RdRp-associated nucleotidyltransferase domain, detailing a new pocket for anti-viral therapeutic development.
External linksbioRxiv / PubMed:32676607 / PubMed Central
MethodsEM (single particle)
Resolution4.0 - 7.9 Å
Structure data

EMDB-22270:
Structure of SARS-CoV-2 replication/transcription complex bound to nsp13 helicase - nsp13(1)-RTC
Method: EM (single particle) / Resolution: 4.0 Å

EMDB-22271:
Structure of SARS-CoV-2 replication/transcription complex bound to nsp13 helicase - (nsp13(2)-RTC)(2)
Method: EM (single particle) / Resolution: 7.9 Å

Source
  • Severe acute respiratory syndrome coronavirus 2

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