Crystal structures of the methyltransferase and helicase from the ZIKA 1947 MR766 Uganda strain.
Bukrejewska, M., Derewenda, U., Radwanska, M., Engel, D.A., Derewenda, Z.S.(2017) Acta Crystallogr D Struct Biol 73: 767-774
- PubMed: 28876240
- DOI: https://doi.org/10.1107/S2059798317010737
- Primary Citation of Related Structures:
5VI7, 5VIM - PubMed Abstract:
Two nonstructural proteins encoded by Zika virus strain MR766 RNA, a methyltransferase and a helicase, were crystallized and their structures were solved and refined at 2.10 and 2.01 Å resolution, respectively. The NS5 methyltransferase contains a bound S-adenosyl-L-methionine (SAM) co-substrate. The NS3 helicase is in the apo form. Comparison with published crystal structures of the helicase in the apo, nucleotide-bound and single-stranded RNA (ssRNA)-bound states suggests that binding of ssRNA to the helicase may occur through conformational selection rather than induced fit.
Organizational Affiliation:
Department of Molecular Physiology and Biological Physics, University of Virginia School of Medicine, Charlottesville, VA 22908-0736, USA.