Ontology highlight
ABSTRACT:
SUBMITTER: Wang B
PROVIDER: S-EPMC5378951 | biostudies-literature | 2017 Mar
REPOSITORIES: biostudies-literature
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]