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Title: Structure of the NS3 helicase from Zika virus

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Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
OSTI Identifier:
Resource Type:
Journal Article
Resource Relation:
Journal Name: Nature Structural & Molecular Biology; Journal Volume: 23; Journal Issue: 8
Country of Publication:
United States

Citation Formats

Jain, Rinku, Coloma, Javier, García-Sastre, Adolfo, and Aggarwal, Aneel K. Structure of the NS3 helicase from Zika virus. United States: N. p., 2016. Web. doi:10.1038/nsmb.3258.
Jain, Rinku, Coloma, Javier, García-Sastre, Adolfo, & Aggarwal, Aneel K. Structure of the NS3 helicase from Zika virus. United States. doi:10.1038/nsmb.3258.
Jain, Rinku, Coloma, Javier, García-Sastre, Adolfo, and Aggarwal, Aneel K. 2016. "Structure of the NS3 helicase from Zika virus". United States. doi:10.1038/nsmb.3258.
title = {Structure of the NS3 helicase from Zika virus},
author = {Jain, Rinku and Coloma, Javier and García-Sastre, Adolfo and Aggarwal, Aneel K.},
abstractNote = {},
doi = {10.1038/nsmb.3258},
journal = {Nature Structural & Molecular Biology},
number = 8,
volume = 23,
place = {United States},
year = 2016,
month = 7
  • Two nonstructural proteins encoded byZika virusstrain MR766 RNA, a methyltransferase and a helicase, were crystallized and their structures were solved and refined at 2.10 and 2.01 Å resolution, respectively. The NS5 methyltransferase contains a boundS-adenosyl-L-methionine (SAM) co-substrate. The NS3 helicase is in the apo form. Comparison with published crystal structures of the helicase in the apo, nucleotide-bound and single-stranded RNA (ssRNA)-bound states suggests that binding of ssRNA to the helicase may occur through conformational selection rather than induced fit.
  • No abstract prepared.
  • The rapid spread of the recentZika virus(ZIKV) epidemic across various countries in the American continent poses a major health hazard for the unborn fetuses of pregnant women. To date, there is no effective medical intervention. The nonstructural protein 5 ofZika virus(ZIKV-NS5) is critical for ZIKV replication through the 5'-RNA capping and RNA polymerase activities present in its N-terminal methyltransferase (MTase) and C-terminal RNA-dependent RNA polymerase (RdRp) domains, respectively. The crystal structure of the full-length ZIKV-NS5 protein has been determined at 3.05 Å resolution from a crystal belonging to space groupP2 12 12 and containing two protein molecules in the asymmetricmore » unit. The structure is similar to that reported for the NS5 protein fromJapanese encephalitis virusand suggests opportunities for structure-based drug design targeting either its MTase or RdRp domain.« less
  • 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. In conclusion, 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 antiviralsmore » for ZIKV.« less