2V8O

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

2V8O の概要

• エントリーDOI: 10.2210/pdb2v8o/pdb
• 分子名称: FLAVIVIRIN PROTEASE NS3 (2 entities in total)
• 機能のキーワード: 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
• 由来する生物種: MURRAY VALLEY ENCEPHALITIS VIRUS
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 49858.59

構造登録者

Mancini, E.J.,Assenberg, R.,Verma, A.,Walter, T.S.,Tuma, R.,Grimes, J.M.,Owens, R.J.,Stuart, D.I. (登録日: 2007-08-09, 公開日: 2007-08-21, 最終更新日: 2023-12-13)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.9 Å)