2f55: Difference between revisions

Revision as of 15:21, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2f55.png

Template:STRUCTURE 2f55

Two hepatitis c virus ns3 helicase domains complexed with the same strand of dnaTwo hepatitis c virus ns3 helicase domains complexed with the same strand of dna

Template:ABSTRACT PUBMED 16306038

About this StructureAbout this Structure

2F55 is a Single protein structure of sequence from Hepatitis c virus. Full crystallographic information is available from OCA.

ReferenceReference

Structural and biological identification of residues on the surface of NS3 helicase required for optimal replication of the hepatitis C virus., Mackintosh SG, Lu JZ, Jordan JB, Harrison MK, Sikora B, Sharma SD, Cameron CE, Raney KD, Sakon J, J Biol Chem. 2006 Feb 10;281(6):3528-35. Epub 2005 Nov 22. PMID:16306038

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Two hepatitis c virus ns3 helicase domains complexed with the same strand of dna'''
+===Two hepatitis c virus ns3 helicase domains complexed with the same strand of dna===
-==Overview==
+<!--
-The hepatitis C virus (HCV) nonstructural protein 3 (NS3) is a multifunctional enzyme with serine protease and DEXH/D-box helicase domains. A crystal structure of the NS3 helicase domain (NS3h) was generated in the presence of a single-stranded oligonucleotide long enough to accommodate binding of two molecules of enzyme. Several amino acid residues at the interface of the two NS3h molecules were identified that appear to mediate a protein-protein interaction between domains 2 and 3 of adjacent molecules. Mutations were introduced into domain 3 to disrupt the putative interface and subsequently examined using an HCV subgenomic replicon, resulting in significant reduction in replication capacity. The mutations in domain 3 were then examined using recombinant NS3h in biochemical assays. The mutant enzyme showed RNA binding and RNA-stimulated ATPase activity that mirrored wild type NS3h. In DNA unwinding assays under single turnover conditions, the mutant NS3h exhibited a similar unwinding rate and only approximately 2-fold lower processivity than wild type NS3h. Overall biochemical activities of the mutant NS3h were similar to the wild type enzyme, which was not reflective of the large reduction in HCV replicative capacity observed in the biological experiment. Hence, the biological results suggest that the known biochemical properties associated with the helicase activity of NS3h do not reveal all of the likely biological roles of NS3 during HCV replication. Domain 3 of NS3 is implicated in protein-protein interactions that are necessary for HCV replication.
+The line below this paragraph, {{ABSTRACT_PUBMED_16306038}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_16306038}}
 ==About this Structure==
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 [[Category: Sakon, J.]]
 [[Category: Hydrolase/dna]]
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