1yks

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[[Image:1yks.gif|left|200px]]
[[Image:1yks.gif|left|200px]]
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{{Structure
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|PDB= 1yks |SIZE=350|CAPTION= <scene name='initialview01'>1yks</scene>, resolution 1.8&Aring;
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The line below this paragraph, containing "STRUCTURE_1yks", creates the "Structure Box" on the page.
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Flavivirin Flavivirin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.91 3.4.21.91] </span>
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{{STRUCTURE_1yks| PDB=1yks | SCENE= }}
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|RELATEDENTRY=[[1ymf|1YMF]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1yks FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yks OCA], [http://www.ebi.ac.uk/pdbsum/1yks PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1yks RCSB]</span>
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'''Crystal structure of yellow fever virus NS3 helicase'''
'''Crystal structure of yellow fever virus NS3 helicase'''
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[[Category: Smith, J L.]]
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Revision as of 13:26, 3 May 2008

Template:STRUCTURE 1yks

Crystal structure of yellow fever virus NS3 helicase


Overview

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.

About this Structure

1YKS is a Single protein structure of sequence from Yellow fever virus. Full crystallographic information is available from OCA.

Reference

Structure of the Flavivirus helicase: implications for catalytic activity, protein interactions, and proteolytic processing., Wu J, Bera AK, Kuhn RJ, Smith JL, J Virol. 2005 Aug;79(16):10268-77. PMID:16051820 Page seeded by OCA on Sat May 3 16:26:46 2008

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