5JWH

Apo structure

5JWH の概要

• エントリーDOI: 10.2210/pdb5jwh/pdb
• 分子名称: NS3 helicase, 1,2-ETHANEDIOL (3 entities in total)
• 機能のキーワード: ntpase, helicase, hydrolase
• 由来する生物種: Zika virus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 51493.60

構造登録者

Cao, X.,Li, Y.,Jin, T. (登録日: 2016-05-12, 公開日: 2016-11-09, 最終更新日: 2023-11-08)

主引用文献

Cao, X.,Li, Y.,Jin, X.,Li, Y.,Guo, F.,Jin, T.
Molecular mechanism of divalent-metal-induced activation of NS3 helicase and insights into Zika virus inhibitor design.
Nucleic Acids Res., 44:10505-10514, 2016

PubMed Abstract: Zika virus has attracted increasing attention because of its potential for causing human neural disorders, including microcephaly in infants and Guillain-Barré syndrome. Its NS3 helicase domain plays critical roles in NTP-dependent RNA unwinding and translocation during viral replication. Our structural analysis revealed a pre-activation state of NS3 helicase in complex with GTPγS, in which the triphosphate adopts a compact conformation in the absence of any divalent metal ions. In contrast, in the presence of a divalent cation, GTPγS adopts an extended conformation, and the Walker A motif undergoes substantial conformational changes. Both features contribute to more extensive interactions between the GTPγS and the enzyme. Thus, this study provides structural evidence on the allosteric modulation of MgNTP on the NS3 helicase activity. Furthermore, the compact conformation of inhibitory NTP identified in this study provides precise information for the rational drug design of small molecule inhibitors for the treatment of ZIKV infection.

PubMed: 27915293
DOI: 10.1093/nar/gkw941

実験手法

X-RAY DIFFRACTION (1.4 Å)