5WXB

crystal structure of ZIKV MTase in complex with SAH

Summary for 5WXB

• Entry DOI: 10.2210/pdb5wxb/pdb
• Descriptor: MRNA cap 0-1 NS5-type MT, S-ADENOSYL-L-HOMOCYSTEINE (3 entities in total)
• Functional Keywords: zika virus, methyltransferase, sah, transferase
• Biological source: Zika virus (strain Mr 766) (ZIKV)
• Cellular location: Virion membrane ; Multi-pass membrane protein : A0A167V0D5
• Total number of polymer chains: 1
• Total formula weight: 29746.96

Authors

Yang, H.,Wang, L.,Zhou, H. (deposition date: 2017-01-07, release date: 2017-05-17, Last modification date: 2024-11-13)

Primary citation

Zhou, H.,Wang, F.,Wang, H.,Chen, C.,Zhang, T.,Han, X.,Wang, D.,Chen, C.,Wu, C.,Xie, W.,Wang, Z.,Zhang, L.,Wang, L.,Yang, H.
The conformational changes of Zika virus methyltransferase upon converting SAM to SAH
Oncotarget, 8:14830-14834, 2017

PubMed Abstract: An outbreak of Zika virus (ZIKV) infection has been reported in South and Central America and the Caribbean. Neonatal microcephaly potentially associated with ZIKV infection has already caused a public health emergency of international concern. Currently, there are no clinically effective vaccines or antiviral drugs available to treat ZIKV infection. The methyltransferase domain (MTase) of ZIKV nonstructural protein 5 (NS5) can sequentially methylate guanine N-7 and ribose 2'-O to form m7NGpppA2'Om cap structure in the new RNA transcripts. This methylation step is crucial for ZIKV replication cycle and evading the host immune system, making it a target for drug design. Here, we present the 1.76 Å crystal structure of ZIKV MTase in complex with the byproduct SAH, providing insight into the elegant methylation process, which will benefit the following antiviral drug development.

PubMed: 28122329
DOI: 10.18632/oncotarget.14780

Experimental method

X-RAY DIFFRACTION (1.762 Å)