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Journal of Virology, August 2005, p. 10268-10277, Vol. 79, No. 16
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.16.10268-10277.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Structure of the Flavivirus Helicase: Implications for Catalytic Activity, Protein Interactions, and Proteolytic Processing

Jinhua Wu,{dagger} Aloke Kumar Bera, Richard J. Kuhn, and Janet L. Smith*

Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907

Received 10 March 2005/ Accepted 27 April 2005

Yellow fever virus (YFV), a member of the Flavivirus genus, has a plus-sense RNA genome encoding a single polyprotein. Viral protein NS3 includes a protease and a helicase that are essential to virus replication and to RNA capping. The 1.8-Å crystal structure of the helicase region of the YFV NS3 protein includes residues 187 to 623. Two familiar helicase domains bind nucleotide in a triphosphate pocket without base recognition, providing a site for nonspecific hydrolysis of nucleoside triphosphates and RNA triphosphate. The third, C-terminal domain has a unique structure and is proposed to function in RNA and protein recognition. The organization of the three domains indicates that cleavage of the viral polyprotein NS3-NS4A junction occurs in trans.

* Corresponding author. Present address: Life Sciences Institute, University of Michigan, 210 Washtenaw Ave., Ann Arbor, MI 48109. Phone: (734) 615-9564. Fax: (734) 763-6492. E-mail: JanetSmith{at}umich.edu.

{dagger} Present address: Skirball Institute of Biomolecular Medicine, New York University School of Medicine, 540 First Avenue, New York, NY 10016.

Journal of Virology, August 2005, p. 10268-10277, Vol. 79, No. 16
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.16.10268-10277.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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