1CU1
CRYSTAL STRUCTURE OF AN ENZYME COMPLEX FROM HEPATITIS C VIRUS
1CU1 の概要
| エントリーDOI | 10.2210/pdb1cu1/pdb |
| 分子名称 | PROTEIN (PROTEASE/HELICASE NS3), ZINC ION, PHOSPHATE ION, ... (4 entities in total) |
| 機能のキーワード | hepatitis c virus, bifunctional, protease-helicase, hydrolase |
| 由来する生物種 | Hepatitis C virus 詳細 |
| 細胞内の位置 | 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 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 137454.42 |
| 構造登録者 | |
| 主引用文献 | Yao, N.,Reichert, P.,Taremi, S.S.,Prosise, W.W.,Weber, P.C. Molecular views of viral polyprotein processing revealed by the crystal structure of the hepatitis C virus bifunctional protease-helicase. Structure Fold.Des., 7:1353-1363, 1999 Cited by PubMed Abstract: Hepatitis C virus (HCV) currently infects approximately 3% of the world's population. HCV RNA is translated into a polyprotein that during maturation is cleaved into functional components. One component, nonstructural protein 3 (NS3), is a 631-residue bifunctional enzyme with protease and helicase activities. The NS3 serine protease processes the HCV polyprotein by both cis and trans mechanisms. The structural aspects of cis processing, the autoproteolysis step whereby the protease releases itself from the polyprotein, have not been characterized. The structural basis for inclusion of protease and helicase activities in a single polypeptide is also unknown. PubMed: 10574797DOI: 10.1016/S0969-2126(00)80025-8 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.5 Å) |
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