2V8O

Structure of the Murray Valley encephalitis virus RNA helicase to 1. 9A resolution

Summary for 2V8O

• Entry DOI: 10.2210/pdb2v8o/pdb
• Descriptor: FLAVIVIRIN PROTEASE NS3 (2 entities in total)
• Functional Keywords: murray valley encephalitis virus, glycoprotein, viral enzymes, transmembrane, cleavage on pair of basic residues, atp-binding, transferase, flaviviridae, core protein, virion, membrane, helicase, hydrolase, helicases, capsid protein, rna replication, envelope protein, nucleotide-binding, nucleotidyltransferase, rna-directed rna polymerase
• Biological source: MURRAY VALLEY ENCEPHALITIS VIRUS
• Total number of polymer chains: 1
• Total formula weight: 49858.59

Authors

Mancini, E.J.,Assenberg, R.,Verma, A.,Walter, T.S.,Tuma, R.,Grimes, J.M.,Owens, R.J.,Stuart, D.I. (deposition date: 2007-08-09, release date: 2007-08-21, Last modification date: 2023-12-13)

Primary citation

Mancini, E.J.,Assenberg, R.,Verma, A.,Walter, T.S.,Tuma, R.,Grimes, J.M.,Owens, R.J.,Stuart, D.I.
Structure of the Murray Valley Encephalitis Virus RNA Helicase at 1.9 A Resolution.
Protein Sci., 16:2294-, 2007

PubMed Abstract: 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.

PubMed: 17893366
DOI: 10.1110/PS.072843107

Experimental method

X-RAY DIFFRACTION (1.9 Å)