1CU1

CRYSTAL STRUCTURE OF AN ENZYME COMPLEX FROM HEPATITIS C VIRUS

Summary for 1CU1

• Entry DOI: 10.2210/pdb1cu1/pdb
• Descriptor: PROTEIN (PROTEASE/HELICASE NS3), ZINC ION, PHOSPHATE ION, ... (4 entities in total)
• Functional Keywords: hepatitis c virus, bifunctional, protease-helicase, hydrolase
• Biological source: Hepatitis C virus; More
• 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: 2
• Total formula weight: 137454.42

Authors

Yao, N.,Weber, P.C. (deposition date: 1999-08-20, release date: 2000-08-23, Last modification date: 2024-02-07)

Primary citation

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

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: 10574797
DOI: 10.1016/S0969-2126(00)80025-8

Experimental method

X-RAY DIFFRACTION (2.5 Å)