7SD4

SARS-CoV-2 Nucleocapsid N-terminal domain (N-NTD) protein

Summary for 7SD4

• Entry DOI: 10.2210/pdb7sd4/pdb
• NMR Information: BMRB: 30955
• Descriptor: Nucleoprotein (1 entity in total)
• Functional Keywords: covid-19, sars-cov-2, nucleocapsid protein, n-terminal domain, rna-binding domain, structural protein
• Biological source: Severe acute respiratory syndrome coronavirus 2 (2019-nCoV, SARS-CoV-2)
• Total number of polymer chains: 1
• Total formula weight: 14994.73

Authors

Sarkar, S.,Runge, B.,Russell, R.W.,Calero, D.,Zeinalilathori, S.,Quinn, C.M.,Lu, M.,Calero, G.,Gronenborn, A.M.,Polenova, T. (deposition date: 2021-09-29, release date: 2022-06-08, Last modification date: 2024-05-15)

Primary citation

Sarkar, S.,Runge, B.,Russell, R.W.,Movellan, K.T.,Calero, D.,Zeinalilathori, S.,Quinn, C.M.,Lu, M.,Calero, G.,Gronenborn, A.M.,Polenova, T.
Atomic-Resolution Structure of SARS-CoV-2 Nucleocapsid Protein N-Terminal Domain.
J.Am.Chem.Soc., 144:10543-10555, 2022

PubMed Abstract: The nucleocapsid (N) protein is one of the four structural proteins of the SARS-CoV-2 virus and plays a crucial role in viral genome organization and, hence, replication and pathogenicity. The N-terminal domain (N) binds to the genomic RNA and thus comprises a potential target for inhibitor and vaccine development. We determined the atomic-resolution structure of crystalline N by integrating solid-state magic angle spinning (MAS) NMR and X-ray diffraction. Our combined approach provides atomic details of protein packing interfaces as well as information about flexible regions as the N- and C-termini and the functionally important RNA binding, β-hairpin loop. In addition, ultrafast (100 kHz) MAS H-detected experiments permitted the assignment of side-chain proton chemical shifts not available by other means. The present structure offers guidance for designing therapeutic interventions against the SARS-CoV-2 infection.

PubMed: 35638584
DOI: 10.1021/jacs.2c03320

Experimental method

SOLID-STATE NMR