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1H, 13C, and 15N backbone and side chain chemical shift assignments of the SARS-CoV-2 non-structural protein 7.
Tonelli, Marco; Rienstra, Chad; Anderson, Thomas K; Kirchdoerfer, Rob; Henzler-Wildman, Katherine.
  • Tonelli M; National Magnetic Resonance Facility at Madison (NMRFAM), University of Wisconsin at Madison, Madison, WI, 53706, USA.
  • Rienstra C; National Magnetic Resonance Facility at Madison (NMRFAM), University of Wisconsin at Madison, Madison, WI, 53706, USA.
  • Anderson TK; Department of Biochemistry, University of Wisconsin at Madison, Madison, WI, 53706, USA.
  • Kirchdoerfer R; National Magnetic Resonance Facility at Madison (NMRFAM), University of Wisconsin at Madison, Madison, WI, 53706, USA.
  • Henzler-Wildman K; Institute for Molecular Virology, University of Wisconsin at Madison, Madison, WI, 53706, USA.
Biomol NMR Assign ; 15(1): 73-77, 2021 04.
Article in English | MEDLINE | ID: covidwho-1141500
ABSTRACT
The SARS-CoV-2 genome encodes for approximately 30 proteins. Within the international project covid19-nmr, we distribute the spectroscopic analysis of the viral proteins and RNA. Here, we report NMR chemical shift assignments for the protein nsp7. The 83 amino acid nsp7 protein is an essential cofactor in the RNA-dependent RNA polymerase. The polymerase activity and processivity of nsp12 are greatly enhanced by binding 1 copy of nsp7 and 2 copies of nsp8 to form a 160 kD complex. A separate hexadecameric complex of nsp7 and nsp8 (8 copies of each) forms a large ring-like structure. Thus, nsp7 is an important component of several large protein complexes that are required for replication of the large and complex coronavirus genome. We here report the near-complete NMR backbone and sidechain resonance assignment (1H,13C,15N) of isolated nsp7 from SARS-CoV-2 in solution. Further, we derive the secondary structure and compare it to the previously reported assignments and structure of the SARS-CoV nsp7.
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Full text: Available Collection: International databases Database: MEDLINE Main subject: Magnetic Resonance Spectroscopy / Coronavirus RNA-Dependent RNA Polymerase / SARS-CoV-2 Language: English Journal: Biomol NMR Assign Journal subject: Molecular Biology / Nuclear Medicine Year: 2021 Document Type: Article Affiliation country: S12104-020-09985-0

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Full text: Available Collection: International databases Database: MEDLINE Main subject: Magnetic Resonance Spectroscopy / Coronavirus RNA-Dependent RNA Polymerase / SARS-CoV-2 Language: English Journal: Biomol NMR Assign Journal subject: Molecular Biology / Nuclear Medicine Year: 2021 Document Type: Article Affiliation country: S12104-020-09985-0