Structure of the Murray Valley encephalitis virus RNA helicase at 1.9 Å resolution

Mancini, Erika J, Assenberg, Rene, Verma, Anil, Walter, Thomas S, Tuma, Roman, Grimes, Jonathan M, Owens, Raymond J and Stuart, David I (2007) Structure of the Murray Valley encephalitis virus RNA helicase at 1.9 Å resolution. Protein Science, 16 (10). pp. 2294-2300. ISSN 0961-8368

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Abstract

Murray Valley encephalitis virus (MVEV), a mosquito-borne flavivirus endemic to Australia, is closely related to Japanese encephalitis virus and West Nile virus. Nonstructural protein 3 (NS3) is a multifunctional enzyme with serine protease and DEXH/D-box helicase domains, whose activity is central to flavivirus replication and is therefore a possible target for anti-flaviviral compounds. Cloning, purification, and crystal structure determination to 1.9 Å resolution of the NS3 helicase of MVEV and characterization of its enzymatic activity is reported. Comparison with the structures of helicases from related viruses supports a possible mechanism of ATP hydrolysis-driven strand separation. Published by Cold Spring Harbor Laboratory Press. Copyright © 2007 The Protein Society.

Item Type: Article
Schools and Departments: School of Life Sciences > Biochemistry
Subjects: Q Science
Depositing User: Tom Gittoes
Date Deposited: 29 Jan 2015 15:39
Last Modified: 29 Jan 2015 15:39
URI: http://sro.sussex.ac.uk/id/eprint/52559
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