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

Hyun Soo Cho, Nam Chul Ha, Lin Woo Kang, Kyung Min Chung, Sung Hoon Back, Sung Key Jang, Byung Ha Oh

Research output: Contribution to journalArticle

177 Citations (Scopus)

Abstract

Crystal structure of RNA helicase domain from genotype 1b hepatitis C virus has been determined at 2.3 Å 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 β-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.

Original languageEnglish
Pages (from-to)15045-15052
Number of pages8
JournalJournal of Biological Chemistry
Volume273
Issue number24
DOIs
Publication statusPublished - 1998 Jun 12

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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