Purification and crystallization of Kokobera virus helicase

De Colibus, L.; Speroni, S.; Coutard, B.; Forrester, N. L.; Gould, E.; Canard, B.; Mattevi, A.. 2007 Purification and crystallization of Kokobera virus helicase. Acta Crystallographica Section F, 63 (3). 193-195. https://doi.org/10.1107/S1744309107005283

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Abstract/Summary

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 P3121 (or P3221), with unit-cell parameters a = 88.6, c = 138.6 Å, and exhibit a diffraction limit of 2.3 Å.

Item Type:	Publication - Article
Digital Object Identifier (DOI):	https://doi.org/10.1107/S1744309107005283
Programmes:	CEH Programmes pre-2009 publications > Biodiversity > BD03 The Genetic Basis of Ecological Function
UKCEH and CEH Sections/Science Areas:	UKCEH Fellows
Format Availability:	Electronic, Print
Additional Keywords:	flaviviruses, helicases, viral replication, arbovirus infections, Queensland, humans
NORA Subject Terms:	Biology and Microbiology Medicine
Date made live:	01 Aug 2007 14:05 +0 (UTC)
URI:	https://nora.nerc.ac.uk/id/eprint/683

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