期刊
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
卷 23, 期 23, 页码 -出版社
MDPI
DOI: 10.3390/ijms232314721
关键词
SARS-CoV-2; NSP13; helicase; RNA; molecular dynamics; HPC
资金
- Ministero dell'Istruzione, dell'Universita e della Ricerca (RFO)
- Consorzio Interuniversitario Risonanze Magnetiche di Metallo Proteine (CIRMMP)
This study compared the structures of NSP13, the essential helicase protein of SARS-CoV-2, in its RNA-free and RNA-engaged forms using molecular dynamics simulations. The results revealed conformational changes and identified the residues responsible for domain-domain interactions in both forms.
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is the causative agent of the pandemic that broke out in 2020 and continues to be the cause of massive global upheaval. Coronaviruses are positive-strand RNA viruses with a genome of similar to 30 kb. The genome is replicated and transcribed by RNA-dependent RNA polymerase together with accessory factors. One of the latter is the protein helicase (NSP13), which is essential for viral replication. The recently solved helicase structure revealed a tertiary structure composed of five domains. Here, we investigated NSP13 from a structural point of view, comparing its RNA-free form with the RNA-engaged form by using atomistic molecular dynamics (MD) simulations at the microsecond timescale. Structural analyses revealed conformational changes that provide insights into the contribution of the different domains, identifying the residues responsible for domain-domain interactions in both observed forms. The RNA-free system appears to be more flexible than the RNA-engaged form. This result underlies the stabilizing role of the nucleic acid and the functional core role of these domains.
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