Crystal structures of the methyltransferase and helicase from the ZIKA 1947 MR766 Uganda strain. Issue 9 (6th September 2017)

• Record Type: Journal Article
• Authors: Bukrejewska, Malgorzata; Derewenda, Urszula; Radwanska, Malwina; Engel, Daniel A.; Derewenda, Zygmunt S.
• Is Part Of: Acta crystallographica. Volume 73:Issue 9(2017)
• Page Start: 767
• Page End: 774
• Publication Date: 2017-09-06
• Subjects: Zika virus -- NS5 methyltransferase -- NS3 helicase -- SAM‐binding stereochemistry; X-ray crystallography -- Periodicals; Crystallography -- Periodicals; Molecular biology -- Periodicals; Molecular structure -- Periodicals; Biomolecules -- Structure -- Periodicals; Cytology -- Periodicals; Biomolecules -- Structure; Crystallography; Cytology; Molecular biology; Molecular structure; X-ray crystallography; Periodicals; 548
• DOI: 10.1107/S2059798317010737
• Languages: English
• ISSNs: 2059-7983

Abstract

Abstract : High‐resolution structures of the Zika virus strain MR766 methyltransferase and helicase proteins are reported. 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.