5U0B

Structure of full-length Zika virus NS5

5U0B の概要

• エントリーDOI: 10.2210/pdb5u0b/pdb
• 関連するPDBエントリー: 5U0C
• 分子名称: Genome polyprotein, S-ADENOSYL-L-HOMOCYSTEINE, ZINC ION, ... (4 entities in total)
• 機能のキーワード: viral rna polymerase, transferase
• 由来する生物種: Zika virus (strain Mr 766) (ZIKV)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 207904.21

構造登録者

Zhao, B.,Du, F. (登録日: 2016-11-23, 公開日: 2017-03-29, 最終更新日: 2024-12-25)

主引用文献

Zhao, B.,Yi, G.,Du, F.,Chuang, Y.C.,Vaughan, R.C.,Sankaran, B.,Kao, C.C.,Li, P.
Structure and function of the Zika virus full-length NS5 protein.
Nat Commun, 8:14762-14762, 2017

PubMed Abstract: The recent outbreak of Zika virus (ZIKV) has infected over 1 million people in over 30 countries. ZIKV replicates its RNA genome using virally encoded replication proteins. Nonstructural protein 5 (NS5) contains a methyltransferase for RNA capping and a polymerase for viral RNA synthesis. Here we report the crystal structures of full-length NS5 and its polymerase domain at 3.0 Å resolution. The NS5 structure has striking similarities to the NS5 protein of the related Japanese encephalitis virus. The methyltransferase contains in-line pockets for substrate binding and the active site. Key residues in the polymerase are located in similar positions to those of the initiation complex for the hepatitis C virus polymerase. The polymerase conformation is affected by the methyltransferase, which enables a more efficiently elongation of RNA synthesis in vitro. Overall, our results will contribute to future studies on ZIKV infection and the development of inhibitors of ZIKV replication.

PubMed: 28345656
DOI: 10.1038/ncomms14762

実験手法

X-RAY DIFFRACTION (3 Å)