甲型肝炎病毒3C蛋白酶：一些特性、结晶及初步晶体学表征

Hepatitis A virus 3C proteinase: some properties, crystallization and preliminary crystallographic characterization.

作者信息

Chernaia M M, Malcolm B A, Allaire M, James M N

机构信息

Department of Biochemistry, University of Alberta, Edmonton, Canada.

出版信息

J Mol Biol. 1993 Dec 5;234(3):890-3. doi: 10.1006/jmbi.1993.1636.

DOI:10.1006/jmbi.1993.1636

PMID:8254682

Abstract

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 The double mutant C24S/C172A of the HAV 3C proteinase, in which both cysteine residues have been replaced by site-directed mutagenesis, was crystallized.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.

摘要

已分离并鉴定了野生型和三种突变型甲型肝炎病毒（HAV）3C蛋白酶的几种同工型。发现活性位点半胱氨酸残基（第172位残基）是其中一些同工型形成的原因。通过定点诱变将两个半胱氨酸残基都替换后的HAV 3C蛋白酶双突变体C24S/C172A被结晶。晶体属于六方空间群P6(1)22（或其对映体P6(5)22），晶胞参数a = b = 65.2 Å，c = 246.1 Å，X射线衍射分辨率为2.3 Å。