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

Mancini Erika J. | Zendy; Assenberg Rene | Zendy; Verma Anil | Zendy; Walter Thomas S. | Zendy; Tuma Roman | Zendy; Grimes Jonathan M. | Zendy; Owens Raymond J. | Zendy; Stuart David I. | Zendy

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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.

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