Hepatitis A virus 3C proteinase: some properties, crystallization and preliminary crystallographic characterization.
Several isoforms of the wild-type and three mutant hepatitis A virus (HAV) 3C proteinases have been isolated and characterized. The active site cysteine residue (residue 172) was found to be responsible for the formation of some of these isoforms. The double mutant C24S/C172A of the HAV 3C proteinase, in which both cysteine residues have been replaced by site-directed mutagenesis, was crystallized. The crystals belong to the hexagonal space group P6(1)22 (or its enantiomorph, P6(5)22) with unit cell dimensions a = b = 65.2 A, c = 246.1 A and diffract X-rays to 2.3 A resolution.
Chernaia
M M
MM
Department of Biochemistry, University of Alberta, Edmonton, Canada.
Malcolm
B A
BA
Allaire
M
M
James
M N
MN
D000086042:3C Viral Proteases; D000595:Amino Acid Sequence; D001665:Binding Sites; D003460:Crystallization; D018360:Crystallography, X-Ray; D003546:Cysteine Endopeptidases / Q000737:chemistry* / Q000302:isolation & purification; D004591:Electrophoresis, Polyacrylamide Gel; D006507:Hepatovirus / Q000201:enzymology*; D007527:Isoenzymes / Q000737:chemistry* / Q000302:isolation & purification; D008970:Molecular Weight; D016297:Mutagenesis, Site-Directed; D017354:Point Mutation; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification; D014764:Viral Proteins
D007527:Isoenzymes; D011994:Recombinant Proteins; D014764:Viral Proteins; D003546:Cysteine Endopeptidases; D000086042:3C Viral Proteases