Bird L E, Hâkansson K, Pan H, Wigley D B
Laboratory of Molecular Biophysics, Rex Richards Building, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Nucleic Acids Res. 1997 Jul 1;25(13):2620-6. doi: 10.1093/nar/25.13.2620.
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.
用谷氨酰胺内切酶Glu-C对噬菌体T7引发酶/解旋酶进行有限的蛋白酶解会产生几个蛋白水解片段。其中一个片段来源于该蛋白质的C端区域，已制备出来并显示保留了解旋酶活性。这一结果支持了一种模型，即基因4蛋白由功能上可分离的结构域组成。已获得该蛋白质C端片段的晶体，适合进行X射线衍射研究。
