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
收藏
页码：2620 / 2626
页数：7
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