7TW8

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

Summary for 7TW8

• Entry DOI: 10.2210/pdb7tw8/pdb
• Descriptor: Transcription factor ETV6,Proofreading exoribonuclease nsp14 chimera, S-ADENOSYL-L-HOMOCYSTEINE, ZINC ION, ... (4 entities in total)
• Functional Keywords: n7-guanine methyl transferase, sars-cov-2, nsp14, viral protein
• Biological source: Severe acute respiratory syndrome coronavirus 2; More
• Total number of polymer chains: 1
• Total formula weight: 35889.08

Authors

Kottur, J.,Aggarwal, A.K. (deposition date: 2022-02-06, release date: 2022-09-07, Last modification date: 2023-10-18)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.55 Å)