7TW8

Structure of nsp14 N7-MethylTransferase domain fused with TELSAM bound to SAH

7TW8 の概要

• エントリーDOI: 10.2210/pdb7tw8/pdb
• 分子名称: Transcription factor ETV6,Proofreading exoribonuclease nsp14 chimera, S-ADENOSYL-L-HOMOCYSTEINE, ZINC ION, ... (4 entities in total)
• 機能のキーワード: n7-guanine methyl transferase, sars-cov-2, nsp14, viral protein
• 由来する生物種: Severe acute respiratory syndrome coronavirus 2; 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35889.08

構造登録者

Kottur, J.,Aggarwal, A.K. (登録日: 2022-02-06, 公開日: 2022-09-07, 最終更新日: 2023-10-18)

主引用文献

Kottur, J.,Rechkoblit, O.,Quintana-Feliciano, R.,Sciaky, D.,Aggarwal, A.K.
High-resolution structures of the SARS-CoV-2 N7-methyltransferase inform therapeutic development.
Nat.Struct.Mol.Biol., 29:850-853, 2022

PubMed Abstract: Emergence of SARS-CoV-2 coronavirus has led to millions of deaths globally. We present three high-resolution crystal structures of the SARS-CoV-2 nsp14 N7-methyltransferase core bound to S-adenosylmethionine (1.62 Å), S-adenosylhomocysteine (1.55 Å) and sinefungin (1.41 Å). We identify features of the methyltransferase core that are crucial for the development of antivirals and show SAH as the best scaffold for the design of antivirals against SARS-CoV-2 and other pathogenic coronaviruses.

PubMed: 36075969
DOI: 10.1038/s41594-022-00828-1

実験手法

X-RAY DIFFRACTION (1.55 Å)