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Protein Science (2007), 16:2294-2300. Published by Cold Spring Harbor Laboratory Press. Copyright © 2007 The Protein Society
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PROTEIN STRUCTURE REPORT

Structure of the Murray Valley encephalitis virus RNA helicase at 1.9 Å resolution

Erika J. Mancini1, Rene Assenberg1, Anil Verma1, Thomas S. Walter1, Roman Tuma2, Jonathan M. Grimes1, Raymond J. Owens1, and David I. Stuart1

1 Division of Structural Biology and Oxford Protein Production Facility, The Henry Wellcome Building for Genomic Medicine, Oxford University, Oxford OX3 7BN, United Kingdom
2 Institute of Biotechnology and Department of Biological and Environmental Sciences, Viikki Biocenter University of Helsinki, Helsinki FIN-00014, Finland

(RECEIVED March 2, 2007; FINAL REVISION June 6, 2007; ACCEPTED June 19, 2007)

Murray 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.

Keywords: Flaviviridae ; Murray Valley encephalitis virus; helicases; viral enzymes


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