A domain of all trades: The enzymatic versatility of the NiRAN domain

Adam Osinski; Vincent S Tagliabracci

doi:10.1016/j.molcel.2023.10.009

A domain of all trades: The enzymatic versatility of the NiRAN domain

Mol Cell. 2023 Nov 2;83(21):3758-3760. doi: 10.1016/j.molcel.2023.10.009.

Authors

Adam Osinski¹, Vincent S Tagliabracci²

Affiliations

¹ Department of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, TX, USA; Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas, TX, USA.
² Department of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, TX, USA; Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas, TX, USA; Harold C. Simmons Comprehensive Cancer Center, University of Texas Southwestern Medical Center, Dallas, TX, USA; Hamon Center for Regenerative Science and Medicine, University of Texas Southwestern Medical Center, Dallas, TX, USA. Electronic address: vincent.tagliabracci@utsouthwestern.edu.

PMID: 37922868
DOI: 10.1016/j.molcel.2023.10.009

Abstract

The SARS-CoV-2 NiRAN domain is essential for viral replication. Despite adopting a pseudokinase fold, it catalyzes three distinct biochemical reactions from a single active site. In this issue of Molecular Cell, Small et al.¹ elucidate the structural intricacies of the NiRAN domain shedding light on the factors that underlie its remarkable versatility.

MeSH terms

Catalytic Domain
SARS-CoV-2*
Virus Replication*