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

journal contribution
posted on 2023-06-08, 19:50 authored by Erika ManciniErika Mancini, Rene Assenberg, Anil Verma, Thomas S Walter, Roman Tuma, Jonathan M Grimes, Raymond J Owens, David I Stuart
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.

History

Publication status

  • Published

Journal

Protein Science

ISSN

0961-8368

Publisher

Wiley-Blackwell

Issue

10

Volume

16

Page range

2294-2300

Department affiliated with

  • Biochemistry Publications

Full text available

  • No

Peer reviewed?

  • Yes

Legacy Posted Date

2015-01-29

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