Purification and crystallization of Kokobera virus helicase

Luigi De Colibus, Silvia Speroni, Bruno Coutard, Naomi L. Forrester, Ernest Gould, Bruno Canard, Andrea Mattevi

Research output: Contribution to journalArticle

5 Scopus citations

Abstract

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

Original languageEnglish (US)
Pages (from-to)193-195
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume63
Issue number3
DOIs
StatePublished - Feb 13 2007

Keywords

  • Flaviviruses
  • Helicases
  • Viral replication

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

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  • Cite this

    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: Structural Biology and Crystallization Communications, 63(3), 193-195. https://doi.org/10.1107/S1744309107005283