7YWR

NMR structure of the N-terminal domain of Nsp8 from SARS-CoV-2

Summary for 7YWR

• Entry DOI: 10.2210/pdb7ywr/pdb
• NMR Information: BMRB: 51325
• Descriptor: ORF1a polyprotein (1 entity in total)
• Functional Keywords: sars-cov-2, non-structural protein, viral protein
• Biological source: Severe acute respiratory syndrome coronavirus 2
• Total number of polymer chains: 1
• Total formula weight: 9336.57

Authors

Mompean, M.,Laurents, D.V.,Pantoja-Uceda, D.,Trevino, M.A. (deposition date: 2022-02-14, release date: 2022-03-02, Last modification date: 2025-01-15)

Primary citation

Trevino, M.A.,Pantoja-Uceda, D.,Laurents, D.V.,Mompean, M.
SARS-CoV-2 Nsp8 N-terminal domain folds autonomously and binds dsRNA.
Nucleic Acids Res., 51:10041-10048, 2023

PubMed Abstract: The SARS-CoV-2 Nsp8 protein is a critical component of the RNA replicase, as its N-terminal domain (NTD) anchors Nsp12, the RNA, and Nsp13. Whereas its C-terminal domain (CTD) structure is well resolved, there is an open debate regarding the conformation adopted by the NTD as it is predicted as disordered but found in a variety of complex-dependent conformations or missing from many other structures. Using NMR spectroscopy, we show that the SARS CoV-2 Nsp8 NTD features both well folded secondary structure and disordered segments. Our results suggest that while part of this domain corresponding to two long α-helices forms autonomously, the folding of other segments would require interaction with other replicase components. When isolated, the α-helix population progressively declines towards the C-termini but surprisingly binds dsRNA while preserving structural disorder.

PubMed: 37665006
DOI: 10.1093/nar/gkad714

Experimental method

SOLUTION NMR