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Structural basis for helicase-polymerase coupling in the SARS-CoV-2 replication-transcription complex.
Chen, James; Malone, Brandon; Llewellyn, Eliza; Grasso, Michael; Shelton, Patrick M M; Olinares, Paul Dominic B; Maruthi, Kashyap; Eng, Ed; Vatandaslar, Hasan; Chait, Brian T; Kapoor, Tarun; Darst, Seth A; Campbell, Elizabeth A.
  • Chen J; Laboratory of Molecular Biophysics, The Rockefeller University, New York, NY, 10065 USA.
  • Malone B; Laboratory of Molecular Biophysics, The Rockefeller University, New York, NY, 10065 USA.
  • Llewellyn E; Laboratory of Molecular Biophysics, The Rockefeller University, New York, NY, 10065 USA.
  • Grasso M; Laboratory of Chemistry and Cell Biology, The Rockefeller University, New York, NY, 10065 USA.
  • Shelton PMM; Laboratory of Chemistry and Cell Biology, The Rockefeller University, New York, NY, 10065 USA.
  • Olinares PDB; Laboratory of Mass Spectrometry and Gaseous Ion Chemistry, The Rockefeller University, New York, NY, 10065 USA.
  • Maruthi K; The National Resource for Automated Molecular Microscopy, Simons Electron Microscopy Center, New York Structural Biology Center, New York, NY, 10027 USA.
  • Eng E; The National Resource for Automated Molecular Microscopy, Simons Electron Microscopy Center, New York Structural Biology Center, New York, NY, 10027 USA.
  • Vatandaslar H; Institute of Molecular Health Sciences, ETH Zurich, 8093 Zürich, Switzerland.
  • Chait BT; Laboratory of Mass Spectrometry and Gaseous Ion Chemistry, The Rockefeller University, New York, NY, 10065 USA.
  • Kapoor T; Laboratory of Chemistry and Cell Biology, The Rockefeller University, New York, NY, 10065 USA.
  • Darst SA; Laboratory of Molecular Biophysics, The Rockefeller University, New York, NY, 10065 USA.
  • Campbell EA; Laboratory of Molecular Biophysics, The Rockefeller University, New York, NY, 10065 USA.
bioRxiv ; 2020 Jul 13.
Article in English | MEDLINE | ID: covidwho-663149
Preprint
This scientific journal article is probably based on a previously available preprint. It has been identified through a machine matching algorithm, human confirmation is still pending.
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ABSTRACT
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.

Full text: Available Collection: International databases Database: MEDLINE Language: English Year: 2020 Document Type: Article

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Full text: Available Collection: International databases Database: MEDLINE Language: English Year: 2020 Document Type: Article