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Comparisons Between the Structures of HCV and Rep Helicases Reveal Structural Similarities Between SF1 and SF2 Super-families of Helicases

Overview
Journal Protein Sci
Specialty Biochemistry
Date 1998 Apr 16
PMID 9541392
Citations 45
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Abstract

Three helicase structures have been determined recently: that of the DNA helicase PcrA, that of the hepatitis C virus RNA helicase, and that of the Escherichia coli DNA helicase Rep. PcrA and Rep belong to the same super-family of helicases (SF1) and are structurally very similar. In contrast, the HCV helicase belongs to a different super-family of helicases, SF2, and shows little sequence homology with the PcrA/Rep helicases. Yet, the HCV helicase is structurally similar to Rep/PcrA, suggesting preservation of structural scaffolds and relationships between helicase motifs across these two super-families. The comparison study presented here also reveals the existence of a new helicase motif in the SF1 family of helicases.

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References
1.
Kim J, Morgenstern K, Lin C, Fox T, Dwyer M, Landro J . Crystal structure of the hepatitis C virus NS3 protease domain complexed with a synthetic NS4A cofactor peptide. Cell. 1996; 87(2):343-55. DOI: 10.1016/s0092-8674(00)81351-3. View

2.
Subramanya H, BIRD L, Brannigan J, Wigley D . Crystal structure of a DExx box DNA helicase. Nature. 1996; 384(6607):379-83. DOI: 10.1038/384379a0. View

3.
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

4.
Story R, Weber I, Steitz T . The structure of the E. coli recA protein monomer and polymer. Nature. 1992; 355(6358):318-25. DOI: 10.1038/355318a0. View

5.
Koonin E, Dolja V . Evolution and taxonomy of positive-strand RNA viruses: implications of comparative analysis of amino acid sequences. Crit Rev Biochem Mol Biol. 1993; 28(5):375-430. DOI: 10.3109/10409239309078440. View