7DE1

Crystal structure of SARS-CoV-2 nucleocapsid protein C-terminal RNA binding domain

7DE1 の概要

• エントリーDOI: 10.2210/pdb7de1/pdb
• 分子名称: Nucleoprotein, DI(HYDROXYETHYL)ETHER (3 entities in total)
• 機能のキーワード: sars-cov-2, nucleocapsid protein, rna binding, c-terminal domain, viral protein
• 由来する生物種: Severe acute respiratory syndrome coronavirus 2 (2019-nCoV)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 26119.30

構造登録者

Chen, S.,Kang, S. (登録日: 2020-11-01, 公開日: 2021-01-27, 最終更新日: 2023-11-29)

主引用文献

Yang, M.,He, S.,Chen, X.,Huang, Z.,Zhou, Z.,Zhou, Z.,Chen, Q.,Chen, S.,Kang, S.
Structural Insight Into the SARS-CoV-2 Nucleocapsid Protein C-Terminal Domain Reveals a Novel Recognition Mechanism for Viral Transcriptional Regulatory Sequences.
Front Chem, 8:624765-624765, 2020

PubMed Abstract: Coronavirus disease 2019 (COVID-19) has caused massive disruptions to society and the economy, and the transcriptional regulatory mechanisms behind the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) are poorly understood. Herein, we determined the crystal structure of the SARS-CoV-2 nucleocapsid protein C-terminal domain (CTD) at a resolution of 2.0 Å, and demonstrated that the CTD has a comparable distinct electrostatic potential surface to equivalent domains of other reported CoVs, suggesting that the CTD has novel roles in viral RNA binding and transcriptional regulation. Further biochemical assays demonstrated that the viral genomic intergenic transcriptional regulatory sequences (TRSs) interact with the SARS-CoV-2 nucleocapsid protein CTD with a flanking region. The unpaired adeno dinucleotide in the TRS stem-loop structure is a major determining factor for their interactions. Taken together, these results suggested that the nucleocapsid protein CTD is responsible for the discontinuous viral transcription mechanism by recognizing the different patterns of viral TRS during transcription.

PubMed: 33511102
DOI: 10.3389/fchem.2020.624765

実験手法

X-RAY DIFFRACTION (2 Å)