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Structural view of the helicase reveals that Zika virus uses a conserved mechanism for unwinding RNA
Author(s) -
Li Lei,
Wang Jin,
Jia Zhihui,
Shaw Neil
Publication year - 2018
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x18003813
Subject(s) - helicase , zika virus , rna helicase a , virology , rna , mechanism (biology) , biology , ns3 , chemistry , computational biology , crystallography , microbiology and biotechnology , virus , genetics , physics , gene , hepatitis c virus , quantum mechanics
Recent studies suggest a link between infection by Zika virus (ZIKV) and the development of neurological complications. The lack of ZIKV‐specific therapeutics has alarmed healthcare professionals worldwide. Here, crystal structures of apo and AMPPNP‐ and Mn 2+ ‐bound forms of the essential helicase of ZIKV refined to 1.78 and 1.3 Å resolution, respectively, are reported. The structures reveal a conserved trimodular topology of the helicase. ATP and Mn 2+ are tethered between two RecA‐like domains by conserved hydrogen‐bonding interactions. The binding of ligands induces the movement of backbone Cα and side‐chain atoms. Numerous solvent molecules are observed in the vicinity of the AMPPNP, suggesting a role in catalysis. These high‐resolution structures could be useful for the design of inhibitors targeting the helicase of ZIKV for the treatment of infections caused by ZIKV.