Crystal structures of the methyltransferase and helicase from the ZIKA 1947 MR766 Uganda strain

摘要

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?? 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.