Literature DB >> 17329812

Purification and crystallization of Kokobera virus helicase.

Luigi De Colibus1, Silvia Speroni, Bruno Coutard, Naomi L Forrester, Ernest Gould, Bruno Canard, Andrea Mattevi.   

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(1)21 (or P3(2)21), with unit-cell parameters a = 88.6, c = 138.6 A, and exhibit a diffraction limit of 2.3 A.

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Year:  2007        PMID: 17329812      PMCID: PMC2330173          DOI: 10.1107/S1744309107005283

Source DB:  PubMed          Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun        ISSN: 1744-3091


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9.  The RNA helicase, nucleotide 5'-triphosphatase, and RNA 5'-triphosphatase activities of Dengue virus protein NS3 are Mg2+-dependent and require a functional Walker B motif in the helicase catalytic core.

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10.  Recombinant protein expression and solubility screening in Escherichia coli: a comparative study.

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  3 in total

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Review 2.  Discovering new medicines targeting helicases: challenges and recent progress.

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