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

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Journal J Virol
Date 2005 Jul 30
PMID 16051820
Citations 74
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Abstract

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-A 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.

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References
1.
Kummerer B, Rice C . Mutations in the yellow fever virus nonstructural protein NS2A selectively block production of infectious particles. J Virol. 2002; 76(10):4773-84. PMC: 136122. DOI: 10.1128/jvi.76.10.4773-4784.2002. View

2.
Yao N, Hesson T, Cable M, Hong Z, Kwong A, Le H . Structure of the hepatitis C virus RNA helicase domain. Nat Struct Biol. 1997; 4(6):463-7. DOI: 10.1038/nsb0697-463. View

3.
Rice C, Lenches E, Eddy S, Shin S, Sheets R, Strauss J . Nucleotide sequence of yellow fever virus: implications for flavivirus gene expression and evolution. Science. 1985; 229(4715):726-33. DOI: 10.1126/science.4023707. View

4.
Yao N, Reichert P, Taremi S, Prosise W, Weber P . Molecular views of viral polyprotein processing revealed by the crystal structure of the hepatitis C virus bifunctional protease-helicase. Structure. 1999; 7(11):1353-63. DOI: 10.1016/s0969-2126(00)80025-8. View

5.
Ishido S, Fujita T, Hotta H . Complex formation of NS5B with NS3 and NS4A proteins of hepatitis C virus. Biochem Biophys Res Commun. 1998; 244(1):35-40. DOI: 10.1006/bbrc.1998.8202. View