5NJV

Flavivirus NS5 domain

5NJV の概要

• エントリーDOI: 10.2210/pdb5njv/pdb
• 分子名称: NS5, S-ADENOSYLMETHIONINE, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: zika, flavivirus, ns5, sah, viral protein
• 由来する生物種: Zika virus (strain Mr 766) (ZIKV)
• 細胞内の位置: Host endoplasmic reticulum membrane ; Peripheral membrane protein ; Lumenal side : A0A146CJG7
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 118048.52

構造登録者

Talapatra, S.K.,Chatrin, C.,Kozielski, F. (登録日: 2017-03-29, 公開日: 2018-01-24, 最終更新日: 2024-11-20)

主引用文献

Chatrin, C.,Talapatra, S.K.,Canard, B.,Kozielski, F.
The structure of the binary methyltransferase-SAH complex from Zika virus reveals a novel conformation for the mechanism of mRNA capping.
Oncotarget, 9:3160-3171, 2018

PubMed Abstract: Zika virus, a flavivirus like Dengue and West Nile viruses, poses a significant risk as a pathogen in the category of emerging infectious diseases. Zika infections typically cause nonspecific, mild symptoms, but can also manifest as a neurological disorder like Guillain-Barré syndrome. Infection in pregnant women is linked to microcephaly in newborn infants. The methyltransferase domain of the non-structural protein 5 is responsible for two sequential methylations of the 5'-RNA cap. This is crucial for genome stability, efficient translation, and escape from the host immune response. Here we present the crystal structures of the Zika methyltransferase domain in complex with the methyl-donor SAM and its by-product SAH. The methyltransferase-SAH binary complex presents a new conformation of a "closed" or "obstructed" state that would restrict the binding of new RNA for capping. The combination and comparison of our new structures with recently published Zika methyltransferase structures provide a first glimpse into the structural mechanism of Zika virus mRNA capping.

PubMed: 29423037
DOI: 10.18632/oncotarget.23223

実験手法

X-RAY DIFFRACTION (2 Å)