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|Title:||Insights into RNA unwinding and ATP hydrolysis by the flavivirus NS3 protein||Authors:||Luo, D.
NS3 helicase structure
|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|
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