Ensemble cryo-EM reveals conformational states of the nsp13 helicase in the SARS-CoV-2 helicase replication-transcription complex.
Autor: | Chen J; Laboratory of Molecular Biophysics, The Rockefeller University, New York, NY, USA., Wang Q; D. E. Shaw Research, New York, NY, USA., Malone B; Laboratory of Molecular Biophysics, The Rockefeller University, New York, NY, USA., Llewellyn E; Laboratory of Molecular Biophysics, The Rockefeller University, New York, NY, USA., Pechersky Y; D. E. Shaw Research, New York, NY, USA., Maruthi K; The National Resource for Automated Molecular Microscopy, Simons Electron Microscopy Center, New York Structural Biology Center, New York, NY, USA., Eng ET; The National Resource for Automated Molecular Microscopy, Simons Electron Microscopy Center, New York Structural Biology Center, New York, NY, USA., Perry JK; Gilead Sciences, Inc., Foster City, CA, USA., Campbell EA; Laboratory of Molecular Biophysics, The Rockefeller University, New York, NY, USA., Shaw DE; D. E. Shaw Research, New York, NY, USA. David.Shaw@DEShawResearch.com.; Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY, USA. David.Shaw@DEShawResearch.com., Darst SA; Laboratory of Molecular Biophysics, The Rockefeller University, New York, NY, USA. darst@rockefeller.edu. |
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Jazyk: | angličtina |
Zdroj: | Nature structural & molecular biology [Nat Struct Mol Biol] 2022 Mar; Vol. 29 (3), pp. 250-260. Date of Electronic Publication: 2022 Mar 08. |
DOI: | 10.1038/s41594-022-00734-6 |
Abstrakt: | The SARS-CoV-2 nonstructural proteins coordinate genome replication and gene expression. Structural analyses revealed the basis for coupling of the essential nsp13 helicase with the RNA-dependent RNA polymerase (RdRp) where the holo-RdRp and RNA substrate (the replication-transcription complex or RTC) associated with two copies of nsp13 (nsp13 (© 2022. The Author(s), under exclusive licence to Springer Nature America, Inc.) |
Databáze: | MEDLINE |
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