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Structure of the Murray Valley encephalitis virus RNA helicase at 1.9 Å resolution
Author(s) -
Mancini Erika J.,
Assenberg Rene,
Verma Anil,
Walter Thomas S.,
Tuma Roman,
Grimes Jonathan M.,
Owens Raymond J.,
Stuart David I.
Publication year - 2007
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.072843107
Subject(s) - helicase , ns3 , flavivirus , virology , biology , virus , rna , biochemistry , hepatitis c virus , gene
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.