5TMH

Structure of Zika virus NS5

Summary for 5TMH

• Entry DOI: 10.2210/pdb5tmh/pdb
• Descriptor: Polyprotein, S-ADENOSYL-L-HOMOCYSTEINE, ZINC ION, ... (5 entities in total)
• Functional Keywords: viral protein
• Biological source: Zika virus (strain Mr 766) (ZIKV)
• Total number of polymer chains: 2
• Total formula weight: 207602.05

Authors

Wang, B.,Tan, X.,Song, J. (deposition date: 2016-10-12, release date: 2017-02-08, Last modification date: 2024-03-06)

Primary citation

Wang, B.,Tan, X.F.,Thurmond, S.,Zhang, Z.M.,Lin, A.,Hai, R.,Song, J.
The structure of Zika virus NS5 reveals a conserved domain conformation.
Nat Commun, 8:14763-14763, 2017

PubMed 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.

PubMed: 28345600
DOI: 10.1038/ncomms14763

Experimental method

X-RAY DIFFRACTION (3.278 Å)