5WZ1

Crystal structure of Zika virus NS5 methyltransferase bound to S-adenosyl-L-methionine

Summary for 5WZ1

• Entry DOI: 10.2210/pdb5wz1/pdb
• Related: 5WZ2 5WZ3
• Descriptor: NS5 methyltransferase, S-ADENOSYLMETHIONINE (2 entities in total)
• Functional Keywords: zika virus, methyltransferase, mtase, sam, transferase
• Biological source: Zika virus (strain Mr 766) (ZIKV)
• Cellular location: Virion membrane ; Multi-pass membrane protein : A0A140E7U5
• Total number of polymer chains: 8
• Total formula weight: 248715.53

Authors

Duan, W.,Song, H.,Qi, J.,Shi, Y.,Gao, G.F. (deposition date: 2017-01-16, release date: 2017-03-08, Last modification date: 2023-11-22)

Primary citation

Duan, W.,Song, H.,Wang, H.,Chai, Y.,Su, C.,Qi, J.,Shi, Y.,Gao, G.F.
The crystal structure of Zika virus NS5 reveals conserved drug targets.
EMBO J., 36:919-933, 2017

PubMed Abstract: Zika virus (ZIKV) has emerged as major health concern, as ZIKV infection has been shown to be associated with microcephaly, severe neurological disease and possibly male sterility. As the largest protein component within the ZIKV replication complex, NS5 plays key roles in the life cycle and survival of the virus through its N-terminal methyltransferase (MTase) and C-terminal RNA-dependent RNA polymerase (RdRp) domains. Here, we present the crystal structures of ZIKV NS5 MTase in complex with an RNA cap analogue (GpppA) and the free NS5 RdRp. We have identified the conserved features of ZIKV NS5 MTase and RdRp structures that could lead to development of current antiviral inhibitors being used against flaviviruses, including dengue virus and West Nile virus, to treat ZIKV infection. These results should inform and accelerate the structure-based design of antiviral compounds against ZIKV.

PubMed: 28254839
DOI: 10.15252/embj.201696241

Experimental method

X-RAY DIFFRACTION (2.507 Å)