Crystal Structures of Flavivirus NS5 Guanylyltransferase Reveal a GMP-Arginine Adduct

Author:

Jia Hengxia12,Zhong Yao12,Peng Chao3,Gong Peng14ORCID

Affiliation:

1. Key Laboratory of Special Pathogens and Biosafety, Wuhan Institute of Virology, Center for Biosafety Mega-Science, Chinese Academy of Sciences, Wuhan, Hubei, China

2. University of Chinese Academy of Sciences, Beijing, China

3. National Facility for Protein Science in Shanghai, Shanghai Advanced Research Institute, Shanghai, China

4. Drug Discovery Center for Infectious Diseases, Nankai University, Tianjin, China

Abstract

The methyltransferase (MTase) domain of flavivirus NS5 is unique in harboring guanylyltransferase (GTase), N7 MTase, and 2′-O MTase activities, playing a central role in viral RNA capping. However, the detailed mechanisms of the multistep capping process remain elusive.

Funder

Ministry of Science and Technology of the People's Republic of China

National Natural Science Foundation of China

Publisher

American Society for Microbiology

Subject

Virology,Insect Science,Immunology,Microbiology

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