Characterization and crystallization of the helicase domain of bacteriophage T7 gene 4 protein

被引：51

作者：

Bird, LE ^{[1
]}

Hakansson, K ^{[1
]}

Pan, H ^{[1
]}

Wigley, DB ^{[1
]}

机构：

[1] UNIV OXFORD,MOL BIOPHYS LAB,OXFORD OX1 3QU,ENGLAND

来源：

NUCLEIC ACIDS RESEARCH | 1997年 / 25卷 / 13期

基金：

英国惠康基金;

关键词：

D O I：

10.1093/nar/25.13.2620

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：

Limited proteolysis of bacteriophage T7 primase/helicase with endoproteinase Glu-C produces several proteolytic fragments. One of these fragments, which is derived from the C-terminal region of the protein, was prepared and shown to retain helicase activity. This result supports a model in which the gene 4 proteins consist of functionally separable domains. Crystals of this C-terminal fragment of the protein have been obtained that are suitable for X-ray diffraction studies.

引用

页码：2620 / 2626

页数：7

共 43 条

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