Journal
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY
Volume 73, Issue -, Pages 767-774Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S2059798317010737
Keywords
Zika virus; NS5 methyltransferase; NS3 helicase; SAM-binding stereochemistry
Funding
- US Department of Energy, Office of Biological and Environmental Research [DE-AC02-06CH11357]
- US Department of Energy [DE-AC02-06CH11357]
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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 angstrom 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.
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