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Structure of the Murray Valley encephalitis virus RNA helicase to 1. 9A resolutionStructure of the Murray Valley encephalitis virus RNA helicase to 1. 9A resolution
Structural highlights
Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedMurray 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. Structure of the Murray Valley encephalitis virus RNA helicase at 1.9 Angstrom resolution.,Mancini EJ, Assenberg R, Verma A, Walter TS, Tuma R, Grimes JM, Owens RJ, Stuart DI Protein Sci. 2007 Oct;16(10):2294-300. PMID:17893366[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Flavivirin
- Large Structures
- Murray valley encephalitis virus
- Assenberg, R
- Grimes, J M
- Mancini, E J
- Owens, R J
- Stuart, D I
- Tuma, R
- Verma, A
- Walter, T S
- Atp-binding
- Capsid protein
- Cleavage on pair of basic residue
- Core protein
- Envelope protein
- Flaviviridae
- Glycoprotein
- Helicase
- Hydrolase
- Membrane
- Nucleotide-binding
- Nucleotidyltransferase
- Rna replication
- Rna-directed rna polymerase
- Transferase
- Transmembrane
- Viral enzyme
- Virion