Structure of the Murray Valley encephalitis virus RNA helicase at 1.9 Å resolution
journal contribution
posted on 2023-06-08, 19:50 authored by Erika ManciniErika Mancini, Rene Assenberg, Anil Verma, Thomas S Walter, Roman Tuma, Jonathan M Grimes, Raymond J Owens, David I StuartMurray Valley encephalitis virus (MVEV), a mosquito-borne flavivirus endemic to Australia, is closely related to Japanese encephalitis virus and West Nile virus. Nonstructural protein 3 (NS3) is a multifunctional enzyme with serine protease and DEXH/D-box helicase domains, whose activity is central to flavivirus replication and is therefore a possible target for anti-flaviviral compounds. Cloning, purification, and crystal structure determination to 1.9 Å resolution of the NS3 helicase of MVEV and characterization of its enzymatic activity is reported. Comparison with the structures of helicases from related viruses supports a possible mechanism of ATP hydrolysis-driven strand separation. Published by Cold Spring Harbor Laboratory Press. Copyright © 2007 The Protein Society.
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- Published
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Protein ScienceISSN
0961-8368Publisher
Wiley-BlackwellExternal DOI
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10Volume
16Page range
2294-2300Department affiliated with
- Biochemistry Publications
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- No
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- Yes
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2015-01-29Usage metrics
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