Purification and crystallization of Kokobera virus helicase

被引:4
作者
De Colibus, Luigi
Speroni, Silvia
Coutard, Bruno
Forrester, Naomi L.
Gould, Ernest
Canard, Bruno
Mattevi, Andrea
机构
[1] Univ Pavia, Dept Genet & Microbiol, I-27100 Pavia, Italy
[2] CNRS, UMR 6098, F-13288 Marseille 09, France
[3] Univ Aix Marseille 1, F-13288 Marseille 09, France
[4] Univ Aix Marseille 2, F-13288 Marseille 09, France
[5] Ctr Ecol & Hydrol, Oxford OX1 3SR, England
[6] Inst Virol, Oxford OX1 3SR, England
来源
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2007年 / 63卷
关键词
D O I
10.1107/S1744309107005283
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Kokobera virus is a mosquito-borne flavivirus belonging, like West Nile virus, to the Japanese encephalitis virus serocomplex. The flavivirus genus is characterized by a positive-sense single-stranded RNA genome. The unique open reading frame of the viral RNA is transcribed and translated as a single polyprotein which is post-translationally cleaved to yield three structural and seven nonstructural proteins, one of which is the NS3 gene that encodes a C-terminal helicase domain consisting of 431 amino acids. Helicase inhibitors are potential antiviral drugs as the helicase is essential to viral replication. Crystals of the Kokobera virus helicase domain were obtained by the hanging-drop vapour-diffusion method. The crystals belong to space group P3(1)21 (or P3(2)21), with unit-cell parameters a = 88.6, c = 138.6 angstrom, and exhibit a diffraction limit of 2.3 angstrom.
引用
收藏
页码:193 / 195
页数:3
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