Please use this identifier to cite or link to this item:
|Title:||Structural insight and flexible features of NS5 proteins from all four serotypes of Dengue virus in solution||Authors:||Saw, Wuan Geok
Subramanian Manimekalai, Malathy Sony
Srinivasan Anand, Ganesh
Weiss, Thomas M.
Vasudevan, Subhash G.
|Keywords:||Biological Sciences||Issue Date:||2015||Source:||Saw, W. G., Tria, G., Grüber, A., Subramanian Manimekalai, M. S., Zhao, Y., Chandramohan, A., et al. (2015). Structural insight and flexible features of NS5 proteins from all four serotypes of Dengue virus in solution . Acta Crystallographica Section D Biological Crystallography, 71(11), 2309-2327.||Series/Report no.:||Acta Crystallographica Section D Biological Crystallography||Abstract:||Infection by the four serotypes of Dengue virus (DENV-1 to DENV-4) causes an important arthropod-borne viral disease in humans. The multifunctional DENV nonstructural protein 5 (NS5) is essential for capping and replication of the viral RNA and harbours a methyltransferase (MTase) domain and an RNA-dependent RNA polymerase (RdRp) domain. In this study, insights into the overall structure and flexibility of the entire NS5 of all four Dengue virus serotypes in solution are presented for the first time. The solution models derived revealed an arrangement of the full-length NS5 (NS5FL) proteins with the MTase domain positioned at the top of the RdRP domain. The DENV-1 to DENV-4 NS5 forms are elongated and flexible in solution, with DENV-4 NS5 being more compact relative to NS5 from DENV-1, DENV-2 and DENV-3. Solution studies of the individual MTase and RdRp domains show the compactness of the RdRp domain as well as the contribution of the MTase domain and the ten-residue linker region to the flexibility of the entire NS5. Swapping the ten-residue linker between DENV-4 NS5FL and DENV-3 NS5FL demonstrated its importance in MTase–RdRp communication and in concerted interaction with viral and host proteins, as probed by amide hydrogen/deuterium mass spectrometry. Conformational alterations owing to RNA binding are presented.||URI:||https://hdl.handle.net/10356/81320
|ISSN:||1399-0047||DOI:||10.1107/S1399004715017721||Schools:||School of Biological Sciences||Rights:||© 2015 International Union of Crystallography. This paper was published in Acta Crystallographica Section D Biological Crystallography and is made available as an electronic reprint (preprint) with permission of International Union of Crystallography. The published version is available at: [http://dx.doi.org/10.1107/S1399004715017721]. One print or electronic copy may be made for personal use only. Systematic or multiple reproduction, distribution to multiple locations via electronic or other means, duplication of any material in this paper for a fee or for commercial purposes, or modification of the content of the paper is prohibited and is subject to penalties under law.||Fulltext Permission:||open||Fulltext Availability:||With Fulltext|
|Appears in Collections:||SBS Journal Articles|
Files in This Item:
|Structural insight and flexible features of NS5 proteins from all four serotypes of Dengue virus in solution.pdf||3.84 MB||Adobe PDF|
Updated on Nov 27, 2023
Web of ScienceTM
Updated on Oct 26, 2023
Updated on Nov 26, 2023
Updated on Nov 26, 2023
Items in DR-NTU are protected by copyright, with all rights reserved, unless otherwise indicated.