Crystal structure of RNA helicase from genotype 1b hepatitis C virus - A feasible mechanism of unwinding duplex RNA

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Crystal structure of RNA helicase domain from genotype 1b hepatitis C virus has been determined at 2.3 Angstrom resolution by the multiple isomorphous replacement method. The structure consists of three domains that form a Y-shaped molecule. One is a NTPase domain containing two highly conserved NTP binding motifs. Another is an RNA binding domain containing a conserved RNA binding motif. The third is a helical domain that contains no beta-strand. The RNA binding domain of the molecule is distinctively separated from the other two domains forming an interdomain cleft into which single stranded RNA can be modeled. A channel is found between a pair of symmetry-related molecules which exhibit the most extensive crystal packing interactions. A stretch of single stranded RNA can be modeled with electrostatic complementarity into the interdomain cleft and continuously through the channel. These observations suggest that some form of this dimer is likely to be the functional form that unwinds double stranded RNA processively by passing one strand of RNA through the channel and passing the other strand outside of the dimer. A "descending molecular see-saw" model is proposed that is consistent with directionality of unwinding and other physicochemical properties of RNA helicases.
Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Issue Date
1998-06
Language
English
Article Type
Article
Keywords

COLI REP HELICASE; NONSTRUCTURAL PROTEIN-3; NS3 PROTEIN; DNA; BINDING; ENZYME; REPLICATION; SEPARATION; CLEAVAGE; ENCODES

Citation

JOURNAL OF BIOLOGICAL CHEMISTRY, v.273, no.24, pp.15045 - 15052

ISSN
0021-9258
DOI
10.1074/jbc.273.24.15045
URI
http://hdl.handle.net/10203/77652
Appears in Collection
BS-Journal Papers(저널논문)
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