1A1Q

HEPATITIS C VIRUS NS3 PROTEINASE

Summary for 1A1Q

• Entry DOI: 10.2210/pdb1a1q/pdb
• Descriptor: NS3 PROTEINASE, ZINC ION (2 entities in total)
• Functional Keywords: hydrolase, serine protease
• 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: 3
• Total formula weight: 59880.04

Authors

Love, R.A.,Parge, H.E.,Wickersham, J.A.,Hostomsky, Z.,Habuka, N.,Moomaw, E.W.,Adachi, T.,Hostomska, Z. (deposition date: 1997-12-12, release date: 1998-03-25, Last modification date: 2024-02-07)

Primary citation

Love, R.A.,Parge, H.E.,Wickersham, J.A.,Hostomsky, Z.,Habuka, N.,Moomaw, E.W.,Adachi, T.,Hostomska, Z.
The crystal structure of hepatitis C virus NS3 proteinase reveals a trypsin-like fold and a structural zinc binding site.
Cell(Cambridge,Mass.), 87:331-342, 1996

PubMed Abstract: During replication of hepatitis C virus (HCV), the final steps of polyprotein processing are performed by a viral proteinase located in the N-terminal one-third of nonstructural protein 3. The structure of NS3 proteinase from HCV BK strain was determined by X-ray crystallography at 2.4 angstrom resolution. NS3P folds as a trypsin-like proteinase with two beta barrels and a catalytic triad of His-57, Asp-81, Ser-139. The structure has a substrate-binding site consistent with the cleavage specificity of the enzyme. Novel features include a structural zinc-binding site and a long N-terminus that interacts with neighboring molecules by binding to a hydrophobic surface patch.

PubMed: 8861916
DOI: 10.1016/S0092-8674(00)81350-1

Experimental method

X-RAY DIFFRACTION (2.4 Å)