5WXB

crystal structure of ZIKV MTase in complex with SAH

5WXB の概要

• エントリーDOI: 10.2210/pdb5wxb/pdb
• 分子名称: MRNA cap 0-1 NS5-type MT, S-ADENOSYL-L-HOMOCYSTEINE (3 entities in total)
• 機能のキーワード: zika virus, methyltransferase, sah, transferase
• 由来する生物種: Zika virus (strain Mr 766) (ZIKV)
• 細胞内の位置: Virion membrane ; Multi-pass membrane protein : A0A167V0D5
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 29746.96

構造登録者

Yang, H.,Wang, L.,Zhou, H. (登録日: 2017-01-07, 公開日: 2017-05-17, 最終更新日: 2023-11-22)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.762 Å)