Unknown

Dataset Information

0

SARS-CoV-2 Nsp8 N-terminal domain folds autonomously and binds dsRNA.


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.

SUBMITTER: Trevino MA 

PROVIDER: S-EPMC10570013 | biostudies-literature | 2023 Oct

REPOSITORIES: biostudies-literature

altmetric image

Publications

SARS-CoV-2 Nsp8 N-terminal domain folds autonomously and binds dsRNA.

Treviño Miguel Á MÁ   Pantoja-Uceda David D   Laurents Douglas V DV   Mompeán Miguel M  

Nucleic acids research 20231001 18


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  ...[more]

Similar Datasets

| S-EPMC7319273 | biostudies-literature
| S-EPMC10163945 | biostudies-literature
| S-SCDT-EMBOR-2021-54322V1 | biostudies-other
| S-EPMC8981793 | biostudies-literature
| S-EPMC2762595 | biostudies-literature
| S-EPMC9173677 | biostudies-literature
| S-EPMC9354780 | biostudies-literature
| S-EPMC8231661 | biostudies-literature
| S-EPMC8238635 | biostudies-literature