1CSJ

CRYSTAL STRUCTURE OF THE RNA-DEPENDENT RNA POLYMERASE OF HEPATITIS C VIRUS

1CSJ の概要

• エントリーDOI: 10.2210/pdb1csj/pdb
• 分子名称: HEPATITIS C VIRUS RNA POLYMERASE (NS5B) (2 entities in total)
• 機能のキーワード: polyprotein, glycoprotein, rna-directed rna polymerase, core protein, coat protein, envelope protein, helicase, atp-binding, transmembrane, nonstructural protein, transferase
• 由来する生物種: Hepatitis C virus
• 細胞内の位置: Core protein p21: Host endoplasmic reticulum membrane; Single-pass membrane protein. Core protein p19: Virion (By similarity). Envelope glycoprotein E1: Virion membrane; Single-pass type I membrane protein (Potential). Envelope glycoprotein E2: Virion membrane; Single-pass type I membrane protein (Potential). p7: Host endoplasmic reticulum membrane; Multi-pass membrane protein (By similarity). Protease NS2-3: Host endoplasmic reticulum membrane; Multi-pass membrane protein (Potential). Serine protease NS3: Host endoplasmic reticulum membrane; Peripheral membrane protein (By similarity). Non-structural protein 4A: Host endoplasmic reticulum membrane; Single-pass type I membrane protein (Potential). Non-structural protein 4B: Host endoplasmic reticulum membrane; Multi-pass membrane protein (By similarity). Non-structural protein 5A: Host endoplasmic reticulum membrane; Peripheral membrane protein (By similarity). RNA-directed RNA polymerase: Host endoplasmic reticulum membrane; Single-pass type I membrane protein (Potential): P26663
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 118892.50

構造登録者

Bressanelli, S.,Tomei, L.,Roussel, A.,Incitti, I.,Vitale, R.L.,Mathieu, M.,De Francesco, R.,Rey, F.A. (登録日: 1999-08-18, 公開日: 1999-11-08, 最終更新日: 2024-11-20)

主引用文献

Bressanelli, S.,Tomei, L.,Roussel, A.,Incitti, I.,Vitale, R.L.,Mathieu, M.,De Francesco, R.,Rey, F.A.
Crystal structure of the RNA-dependent RNA polymerase of hepatitis C virus.
Proc.Natl.Acad.Sci.USA, 96:13034-13039, 1999

PubMed Abstract: We report the crystal structure of the RNA-dependent RNA polymerase of hepatitis C virus, a major human pathogen, to 2.8-A resolution. This enzyme is a key target for developing specific antiviral therapy. The structure of the catalytic domain contains 531 residues folded in the characteristic fingers, palm, and thumb subdomains. The fingers subdomain contains a region, the "fingertips," that shares the same fold with reverse transcriptases. Superposition to the available structures of the latter shows that residues from the palm and fingertips are structurally equivalent. In addition, it shows that the hepatitis C virus polymerase was crystallized in a closed fingers conformation, similar to HIV-1 reverse transcriptase in ternary complex with DNA and dTTP [Huang H., Chopra, R., Verdine, G. L. & Harrison, S. C. (1998) Science 282, 1669-1675]. This superposition reveals the majority of the amino acid residues of the hepatitis C virus enzyme that are likely to be implicated in binding to the replicating RNA molecule and to the incoming NTP. It also suggests a rearrangement of the thumb domain as well as a possible concerted movement of thumb and fingertips during translocation of the RNA template-primer in successive polymerization rounds.

PubMed: 10557268
DOI: 10.1073/pnas.96.23.13034

実験手法

X-RAY DIFFRACTION (2.8 Å)