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

176 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

Fingerprint

RNA Helicases
Viruses
Hepacivirus
Crystal structure
Genotype
RNA
Nucleoside-Triphosphatase
Double-Stranded RNA
Static Electricity
Dimers
Molecules
Crystal symmetry
RNA-Binding Motifs
Electrostatics
Crystals

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Cho, Hyun Soo ; Ha, Nam Chul ; Kang, Lin Woo ; Chung, Kyung Min ; Back, Sung Hoon ; Jang, Sung Key ; Oh, Byung Ha. / Crystal structure of RNA helicase from genotype 1b hepatitis C virus. A feasible mechanism of unwinding duplex RNA. In: Journal of Biological Chemistry. 1998 ; Vol. 273, No. 24. pp. 15045-15052.
@article{70948cd8eb3f465180edf5dad468c826,
title = "Crystal structure of RNA helicase from genotype 1b hepatitis C virus. A feasible mechanism of unwinding duplex RNA",
abstract = "Crystal structure of RNA helicase domain from genotype 1b hepatitis C virus has been determined at 2.3 {\AA} 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.",
author = "Cho, {Hyun Soo} and Ha, {Nam Chul} and Kang, {Lin Woo} and Chung, {Kyung Min} and Back, {Sung Hoon} and Jang, {Sung Key} and Oh, {Byung Ha}",
year = "1998",
month = "6",
day = "12",
doi = "10.1074/jbc.273.24.15045",
language = "English",
volume = "273",
pages = "15045--15052",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "24",

}

Crystal structure of RNA helicase from genotype 1b hepatitis C virus. A feasible mechanism of unwinding duplex RNA. / Cho, Hyun Soo; Ha, Nam Chul; Kang, Lin Woo; Chung, Kyung Min; Back, Sung Hoon; Jang, Sung Key; Oh, Byung Ha.

In: Journal of Biological Chemistry, Vol. 273, No. 24, 12.06.1998, p. 15045-15052.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Crystal structure of RNA helicase from genotype 1b hepatitis C virus. A feasible mechanism of unwinding duplex RNA

AU - Cho, Hyun Soo

AU - Ha, Nam Chul

AU - Kang, Lin Woo

AU - Chung, Kyung Min

AU - Back, Sung Hoon

AU - Jang, Sung Key

AU - Oh, Byung Ha

PY - 1998/6/12

Y1 - 1998/6/12

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0032510963&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0032510963&partnerID=8YFLogxK

U2 - 10.1074/jbc.273.24.15045

DO - 10.1074/jbc.273.24.15045

M3 - Article

C2 - 9614113

AN - SCOPUS:0032510963

VL - 273

SP - 15045

EP - 15052

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 24

ER -