2BHR

Dengue virus RNA helicase

2BHR の概要

• エントリーDOI: 10.2210/pdb2bhr/pdb
• 分子名称: RNA HELICASE, SULFATE ION (3 entities in total)
• 機能のキーワード: hydrolase, helicase, nucleoside triphosphatase, rna-replication
• 由来する生物種: DENGUE VIRUS 2
• 細胞内の位置: Envelope protein E: Virion membrane; Multi- pass membrane protein: Q91H74
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 103442.19

構造登録者

Xu, T.,Sampath, A.,Chao, A.,Wen, D.,Nanao, M.,Chene, P.,Vasudevan, S.G.,Lescar, J. (登録日: 2005-01-17, 公開日: 2005-08-03, 最終更新日: 2024-05-08)

主引用文献

Xu, T.,Sampath, A.,Chao, A.,Wen, D.,Nanao, M.,Chene, P.,Vasudevan, S.G.,Lescar, J.
Structure of the Dengue Virus Helicase/Nucleoside Triphosphatase Catalytic Domain at a Resolution of 2.4 A.
J.Virol., 79:10278-, 2005

PubMed Abstract: Dengue fever is an important emerging public health concern, with several million viral infections occurring annually, for which no effective therapy currently exists. The NS3 protein from Dengue virus is a multifunctional protein of 69 kDa, endowed with protease, helicase, and nucleoside 5'-triphosphatase (NTPase) activities. Thus, NS3 plays an important role in viral replication and represents a very interesting target for the development of specific antiviral inhibitors. We present the structure of an enzymatically active fragment of the Dengue virus NTPase/helicase catalytic domain to 2.4 A resolution. The structure is composed of three domains, displays an asymmetric distribution of charges on its surface, and contains a tunnel large enough to accommodate single-stranded RNA. Its C-terminal domain adopts a new fold compared to the NS3 helicase of hepatitis C virus, which has interesting implications for the evolution of the Flaviviridae replication complex. A bound sulfate ion reveals residues involved in the metal-dependent NTPase catalytic mechanism. Comparison with the NS3 hepatitis C virus helicase complexed to single-stranded DNA would place the 3' single-stranded tail of a nucleic acid duplex in the tunnel that runs across the basic face of the protein. A possible model for the unwinding mechanism is proposed.

PubMed: 16051821
DOI: 10.1128/JVI.79.16.10278-10288.2005

実験手法

X-RAY DIFFRACTION (2.8 Å)