HEPATITIS-A VIRUS 3C-PROTEINASE - SOME PROPERTIES, CRYSTALLIZATION AND PRELIMINARY CRYSTALLOGRAPHIC CHARACTERIZATION

被引：9

作者：

CHERNAIA, MM

MALCOLM, BA

ALLAIRE, M

JAMES, MNG

机构：

[1] MRC Group in Protein Structure and Function, Department of Biochemistry, University of Alberta, Edmonton

[2] Department of Biochemistry, Department of Medical Microbiology and Infectious Diseases, University of Alberta, Edmonton

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1993年 / 234卷 / 03期

关键词：

HAV; 3C-PROTEINASE; MUTANTS; PICORNAVIRAL PROTEINASES; CRYSTALLIZATION;

D O I：

10.1006/jmbi.1993.1636

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 The double mutant C24S/CI72A of the HAV 3C proteinase, in which both cysteine residues have been replaced by site-directed mutagenesis, was crystallized.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 P6122 (or its enantiomorph, P6522) with unit cell dimensions a = b = 65.2 Å, c = 246.1 Å and diffract X-rays to 2.3 Å resolution. © 1993 Academic Press Limited.

引用

页码：890 / 893

页数：4

共 13 条

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