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The structure of Zika virus NS5 reveals a conserved domain conformation.


ABSTRACT: The recent outbreak of Zika virus (ZIKV) has imposed a serious threat to public health. Here we report the crystal structure of the ZIKV NS5 protein in complex with S-adenosyl-L-homocysteine, in which the tandem methyltransferase (MTase) and RNA-dependent RNA polymerase (RdRp) domains stack into one of the two alternative conformations of flavivirus NS5 proteins. The activity of this NS5 protein is verified through a de novo RdRp assay on a subgenomic ZIKV RNA template. Importantly, our structural analysis leads to the identification of a potential drug-binding site of ZIKV NS5, which might facilitate the development of novel antivirals for ZIKV.

SUBMITTER: Wang B 

PROVIDER: S-EPMC5378951 | biostudies-literature | 2017 Mar

REPOSITORIES: biostudies-literature

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The structure of Zika virus NS5 reveals a conserved domain conformation.

Wang Boxiao B   Tan Xiao-Feng XF   Thurmond Stephanie S   Zhang Zhi-Min ZM   Lin Asher A   Hai Rong R   Song Jikui J  

Nature communications 20170327


The recent outbreak of Zika virus (ZIKV) has imposed a serious threat to public health. Here we report the crystal structure of the ZIKV NS5 protein in complex with S-adenosyl-L-homocysteine, in which the tandem methyltransferase (MTase) and RNA-dependent RNA polymerase (RdRp) domains stack into one of the two alternative conformations of flavivirus NS5 proteins. The activity of this NS5 protein is verified through a de novo RdRp assay on a subgenomic ZIKV RNA template. Importantly, our structur  ...[more]

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