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dc.contributor.author
Chen, James
dc.contributor.author
Malone, Brandon
dc.contributor.author
Llewellyn, Eliza
dc.contributor.author
Grasso, Michael
dc.contributor.author
Shelton, Patrick M.M.
dc.contributor.author
Olinares, Paul D.B.
dc.contributor.author
Maruthi, Kashyap
dc.contributor.author
Eng, Edward T.
dc.contributor.author
Vatandaslar, Hasan
dc.contributor.author
Chait, Brian T.
dc.contributor.author
Kapoor, Tarun M.
dc.contributor.author
Darst, Seth A.
dc.contributor.author
Campbell, Elizabeth A.
dc.date.accessioned
2020-09-21T11:07:12Z
dc.date.available
2020-09-20T04:25:40Z
dc.date.available
2020-09-21T11:07:12Z
dc.date.issued
2020-09-17
dc.identifier.issn
0092-8674
dc.identifier.issn
1097-4172
dc.identifier.other
10.1016/j.cell.2020.07.033
en_US
dc.identifier.uri
http://hdl.handle.net/20.500.11850/441334
dc.description.abstract
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/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 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-Mg2+ bound in the nsp12 N-terminal nidovirus RdRp-associated nucleotidyltransferase domain, detailing a new pocket for anti-viral therapy development. © 2020 Elsevier Inc.
en_US
dc.language.iso
en
en_US
dc.publisher
Cell Press
en_US
dc.title
Structural Basis for Helicase-Polymerase Coupling in the SARS-CoV-2 Replication-Transcription Complex
en_US
dc.type
Journal Article
dc.date.published
2020-07-28
ethz.journal.title
Cell
ethz.journal.volume
182
en_US
ethz.journal.issue
6
en_US
ethz.journal.abbreviated
Cell
ethz.pages.start
1560
en_US
ethz.pages.end
1573.e13
en_US
ethz.identifier.wos
ethz.identifier.scopus
ethz.publication.place
Cambridge, MA
en_US
ethz.publication.status
published
en_US
ethz.date.deposited
2020-09-20T04:26:59Z
ethz.source
SCOPUS
ethz.eth
yes
en_US
ethz.availability
Metadata only
en_US
ethz.rosetta.installDate
2020-09-21T11:07:26Z
ethz.rosetta.lastUpdated
2024-02-02T12:07:15Z
ethz.rosetta.versionExported
true
ethz.COinS
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