7O35

Crystal Structure of SARS-CoV-2 N-CTD in complex with GTP (I)

7O35 の概要

• エントリーDOI: 10.2210/pdb7o35/pdb
• 分子名称: Nucleoprotein, GUANOSINE-5'-TRIPHOSPHATE (3 entities in total)
• 機能のキーワード: nucleocapsid, viral protein
• 由来する生物種: Severe acute respiratory syndrome coronavirus 2 (2019-nCoV, SARS-CoV-2)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 62083.98

構造登録者

Ciges-Tomas, J.R.,Vilar, M. (登録日: 2021-04-01, 公開日: 2022-04-13, 最終更新日: 2024-01-31)

主引用文献

Rafael Ciges-Tomas, J.,Franco, M.L.,Vilar, M.
Identification of a guanine-specific pocket in the protein N of SARS-CoV-2.
Commun Biol, 5:711-711, 2022

PubMed Abstract: The SARS-CoV-2 nucleocapsid protein (N) is responsible for RNA binding. Here we report the crystal structure of the C-terminal domain (N) in open and closed conformations and in complex with guanine triphosphate, GTP. The crystal structure and biochemical studies reveal a specific interaction between the guanine, a nucleotide enriched in the packaging signals regions of coronaviruses, and a highly conserved tryptophan residue (W330). In addition, EMSA assays with SARS-CoV-2 derived RNA hairpin loops from a putative viral packaging sequence showed the preference interaction of the N-CTD to RNA oligonucleotides containing G and the loss of the specificity in the mutant W330A. Here we propose that this interaction may facilitate the viral assembly process. In summary, we have identified a specific guanine-binding pocket in the N protein that may be used to design viral assembly inhibitors.

PubMed: 35842466
DOI: 10.1038/s42003-022-03647-8

実験手法

X-RAY DIFFRACTION (1.8 Å)