2v8o
From Proteopedia
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| , resolution 1.90Å | |||||||
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| Activity: | Flavivirin, with EC number 3.4.21.91 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF THE MURRAY VALLEY ENCEPHALITIS VIRUS RNA HELICASE TO 1.9A RESOLUTION
Overview
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.
About this Structure
2V8O is a Single protein structure of sequence from Murray valley encephalitis virus. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Mon Mar 31 05:09:35 2008
Categories: Flavivirin | Murray valley encephalitis virus | Single protein | 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
