8OHM
CRYSTAL STRUCTURE OF RNA HELICASE FROM GENOTYPE 1B HEPATITIS C VIRUS: MECHANISM OF UNWINDING DUPLEX RNA
Summary for 8OHM
| Entry DOI | 10.2210/pdb8ohm/pdb |
| Descriptor | RNA HELICASE (2 entities in total) |
| Functional Keywords | rna helicase, hepatitis c virus, hcv, unwinding mechanism, helicase |
| Biological source | Hepatitis C virus |
| Cellular location | Core protein p21: Host endoplasmic reticulum membrane; Single-pass membrane protein. Core protein p19: Virion . Envelope glycoprotein E1: Virion membrane ; Single-pass type I membrane protein . Envelope glycoprotein E2: Virion membrane ; Single-pass type I membrane protein . p7: Host endoplasmic reticulum membrane ; Multi-pass membrane protein . Protease NS2-3: Host endoplasmic reticulum membrane ; Multi-pass membrane protein . Serine protease NS3: Host endoplasmic reticulum membrane ; Peripheral membrane protein . Non-structural protein 4A: Host endoplasmic reticulum membrane ; Single-pass type I membrane protein . Non-structural protein 4B: Host endoplasmic reticulum membrane ; Multi-pass membrane protein . Non-structural protein 5A: Host endoplasmic reticulum membrane ; Peripheral membrane protein . RNA-directed RNA polymerase: Host endoplasmic reticulum membrane ; Single-pass type I membrane protein : P26663 |
| Total number of polymer chains | 1 |
| Total formula weight | 46602.85 |
| Authors | Cho, H.S.,Ha, N.C.,Kang, L.W.,Oh, B.H. (deposition date: 1998-03-13, release date: 1999-04-20, Last modification date: 2024-02-14) |
| Primary citation | Cho, H.S.,Ha, N.C.,Kang, L.W.,Chung, K.M.,Back, S.H.,Jang, S.K.,Oh, B.H. Crystal structure of RNA helicase from genotype 1b hepatitis C virus. A feasible mechanism of unwinding duplex RNA. J.Biol.Chem., 273:15045-15052, 1998 Cited by PubMed Abstract: Crystal structure of RNA helicase domain from genotype 1b hepatitis C virus has been determined at 2.3 A 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. PubMed: 9614113DOI: 10.1074/jbc.273.24.15045 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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