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PDBsum entry 2v8o
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References listed in PDB file
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Key reference
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Title
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Structure of the murray valley encephalitis virus RNA helicase at 1.9 a resolution.
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Authors
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E.J.Mancini,
R.Assenberg,
A.Verma,
T.S.Walter,
R.Tuma,
J.M.Grimes,
R.J.Owens,
D.I.Stuart.
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Ref.
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Protein Sci, 2007,
16,
2294-2300.
[DOI no: ]
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PubMed id
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Abstract
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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 A
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.
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Figure 2.
Figure 2. (A) The structures of MVEVh (yellow) and YFVh (blue) superimposed via domain 3 (superimposition performed using
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The above figure is
reprinted
by permission from the Protein Society:
Protein Sci
(2007,
16,
2294-2300)
copyright 2007.
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