PDBsum entry 7de1

Viral protein

PDB id: 7de1

Contents

Protein chains

108 a.a.

115 a.a.

Ligands

PEG ×3

Waters ×240

PDB id:

7de1

Name:

Viral protein

Title:

Crystal structure of sars-cov-2 nucleocapsid protein c-terminal RNA binding domain

Structure:

Nucleoprotein. Chain: a, b. Fragment: c-terminal RNA binding domain. Synonym: n,nucleocapsid protein,protein n. Engineered: yes

Source:

Severe acute respiratory syndrome coronavirus 2. 2019-ncov. Organism_taxid: 2697049. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.00Å R-factor: 0.177 R-free: 0.223

Authors:

S.Chen,S.Kang

Key ref:

M.Yang et al. (2020). 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. PubMed id: 33511102 DOI: 10.3389/fchem.2020.624765

Date:

01-Nov-20 Release date: 27-Jan-21

Protein chain

P0DTC9  (NCAP_SARS2) -  Nucleoprotein from Severe acute respiratory syndrome coronavirus 2

Seq: 419 a.a.

Struc: 108 a.a.

Protein chain

P0DTC9  (NCAP_SARS2) -  Nucleoprotein from Severe acute respiratory syndrome coronavirus 2

Seq: 419 a.a.

Struc: 115 a.a.

DOI no: 10.3389/fchem.2020.624765

Front Chem 8:624765 (2020)

PubMed id: 33511102

Structural Insight Into the SARS-CoV-2 Nucleocapsid Protein C-Terminal Domain Reveals a Novel Recognition Mechanism for Viral Transcriptional Regulatory Sequences.

M.Yang, S.He, X.Chen, Z.Huang, Z.Zhou, Z.Zhou, Q.Chen, S.Chen, S.Kang.

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 in vitro 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.