7L1F

SARS-CoV-2 RdRp in complex with 4 Remdesivir monophosphate

Summary for 7L1F

• Entry DOI: 10.2210/pdb7l1f/pdb
• EMDB information: 23109
• Descriptor: RNA-directed RNA polymerase, Non-structural protein 8, Non-structural protein 7, ... (5 entities in total)
• Functional Keywords: viral protein, viral protein-rna complex, viral protein/rna
• Biological source: Severe acute respiratory syndrome coronavirus 2 (2019-nCoV, SARS-CoV-2); More
• Total number of polymer chains: 5
• Total formula weight: 134214.74

Authors

Bravo, J.P.K.,Taylor, D.W. (deposition date: 2020-12-14, release date: 2021-02-10, Last modification date: 2024-03-06)

Primary citation

Bravo, J.P.K.,Dangerfield, T.L.,Taylor, D.W.,Johnson, K.A.
Remdesivir is a delayed translocation inhibitor of SARS-CoV-2 replication.
Mol.Cell, 81:1548-1552.e4, 2021

PubMed Abstract: Remdesivir is a nucleoside analog approved by the US FDA for treatment of COVID-19. Here, we present a 3.9-Å-resolution cryo-EM reconstruction of a remdesivir-stalled RNA-dependent RNA polymerase complex, revealing full incorporation of 3 copies of remdesivir monophosphate (RMP) and a partially incorporated fourth RMP in the active site. The structure reveals that RMP blocks RNA translocation after incorporation of 3 bases following RMP, resulting in delayed chain termination, which can guide the rational design of improved antiviral drugs.

PubMed: 33631104
DOI: 10.1016/j.molcel.2021.01.035

Experimental method

ELECTRON MICROSCOPY (3.89 Å)