Please use this identifier to cite or link to this item: https://doi.org/10.1038/emboj.2008.232
Title: Insights into RNA unwinding and ATP hydrolysis by the flavivirus NS3 protein
Authors: Luo, D.
Xu, T.
Watson, R.P.
Scherer-Becker, D.
Sampath, A.
Jahnke, W.
Yeong, S.S.
Wang, C.H.
Lim, S.P.
Strongin, A.
Vasudevan, S.G. 
Lescar, J.
Keywords: ATP analogues
Dengue virus
Flaviviruses
NS3 helicase structure
RNA complex
Issue Date: 3-Dec-2008
Citation: Luo, D., Xu, T., Watson, R.P., Scherer-Becker, D., Sampath, A., Jahnke, W., Yeong, S.S., Wang, C.H., Lim, S.P., Strongin, A., Vasudevan, S.G., Lescar, J. (2008-12-03). Insights into RNA unwinding and ATP hydrolysis by the flavivirus NS3 protein. EMBO Journal 27 (23) : 3209-3219. ScholarBank@NUS Repository. https://doi.org/10.1038/emboj.2008.232
Abstract: Together with the NS5 polymerase, the NS3 helicase has a pivotal function in flavivirus RNA replication and constitutes an important drug target. We captured the dengue virus NS3 helicase at several stages along the catalytic pathway including bound to single-stranded (ss) RNA, to an ATP analogue, to a transition-state analogue and to ATP hydrolysis products. RNA recognition appears largely sequence independent in a way remarkably similar to eukaryotic DEAD box proteins Vasa and eIF4AIII. On ssRNA binding, the NS3 enzyme switches to a catalytic-competent state imparted by an inward movement of the P-loop, interdomain closure and a change in the divalent metal coordination shell, providing a structural basis for RNA-stimulated ATP hydrolysis. These structures demonstrate for the first time large quaternary changes in the flaviviridae helicase, identify the catalytic water molecule and point to a β-hairpin that protrudes from subdomain 2, as a critical element for dsRNA unwinding. They also suggest how NS3 could exert an effect as an RNA-anchoring device and thus participate both in flavivirus RNA replication and assembly. ©2008 European Molecular Biology Organization.
Source Title: EMBO Journal
URI: http://scholarbank.nus.edu.sg/handle/10635/110139
ISSN: 02614189
DOI: 10.1038/emboj.2008.232
Appears in Collections:Staff Publications

Show full item record
Files in This Item:
There are no files associated with this item.

SCOPUSTM   
Citations

193
checked on Nov 29, 2022

WEB OF SCIENCETM
Citations

171
checked on Sep 28, 2021

Page view(s)

110
checked on Nov 24, 2022

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.