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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 Angstrom 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.

Original publication

DOI

10.1110/ps.072843107

Type

Journal article

Journal

Protein Sci

Publication Date

10/2007

Volume

16

Pages

2294 - 2300

Keywords

Adenosine Triphosphatases, Amino Acid Motifs, Amino Acid Sequence, Crystallography, X-Ray, Encephalitis Virus, Murray Valley, Models, Molecular, Molecular Sequence Data, Nucleotides, RNA Helicases, Sequence Alignment, Serine Endopeptidases, Viral Nonstructural Proteins