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. 2016 Aug;23(8):752-4.
doi: 10.1038/nsmb.3258. Epub 2016 Jul 11.

Structure of the NS3 helicase from Zika virus

Rinku Jain  1 , Javier Coloma  1 , Adolfo García-Sastre  2   3   4 , Aneel K Aggarwal  1
Affiliations

Structure of the NS3 helicase from Zika virus

Rinku Jain et al. Nat Struct Mol Biol. 2016 Aug.

Abstract

Zika virus has emerged as a pathogen of major health concern. Here, we present a high-resolution (1.62-Å) crystal structure of the RNA helicase from the French Polynesia strain. The structure is similar to that of the RNA helicase from Dengue virus, with variability in the conformations of loops typically involved in binding ATP and RNA. We identify druggable 'hotspots' that are well suited for in silico and/or fragment-based high-throughput drug discovery.

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Figures

Figure 1
Figure 1
Structure comparison of ZIKV NS3-Hel with DENV4 NS3 helicase. Overall fold of ZIKV NS3-Hel residues 171:617 (left) and DENV4 helicase (PDB ID 2JLQ, right). RecA like domains 1 and 2 are colored green and cyan, and domain 3 is colored orange. ATP binding pocket and RNA binding groove are indicated.
Figure 2
Figure 2
Features of the ZIKV NS3-Hel structure. (a) Difference electron density (contoured at 3σ) near the P-loop. Magnified view is shown on the right. Residues of the P-loop in the vicinity of the density are shown in tan stick, modeled pyrophosphate (PPi) is shown as orange stick. (b) Superimposition of ZIKV NS3-Hel with DENV4 NS3-Hel via domain 1. Domain 3 has been omitted for clarity. ZIKV NS3-Hel is shown in tan with the P-loop and RNA binding loop in red, and for the DENV4 helicase in cyan and blue respectively.
Figure 3
Figure 3
Hot spots predicted by FTmap for ZIKV NS3-Hel domain. Eleven hot spots predicted by FTmap are shown in grey mesh, and the cluster of probes at each spot shown as sticks of various colors. These hot spots coalesce into two broad and contiguous sites that map between domains 1 and 2 (site 1) and at the confluence of domains 1 and 3 (site 2).
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