Novel structure of an N-terminal domain that is crucial for the dimeric assembly and DNA-binding of an archaeal DNA polymerase D large subunit from Pyrococcus horikoshii
Novel structure of an N-terminal domain that is crucial for the dimeric assembly and DNA-binding of an archaeal DNA polymerase D large subunit from Pyrococcus horikoshii
复制标题
DOI：
10.1016/j.febslet.2010.12.040
复制
发表时间：
2011-02-04
期刊：
影响因子：
3.5
通讯作者：
Yokoyama, Hideshi
中科院分区：
文献类型：
--
作者：
Matsui, Ikuo;Urushibata, Yuji;Yokoyama, Hideshi
大肠杆菌特异性D家族DNA聚合酶形成由两个大的聚合酶亚基和两个小的核酸外切酶亚基组成的异源四聚体。通过X射线晶体学测定大亚基的N-末端（1-300）结构域结构，尽管类似于50个N-末端残基是无序的。确定的结构由九个α螺旋和三个β链组成。我们还通过SPR测量鉴定了该结构域的DNA结合能力。N-末端（1-100）区域通过将类似于50个N-末端残基与它们自己的催化区域（792-1163）连接而在大亚基二聚体的折叠中起着至关重要的作用。结构化概要：DP 2通过分子筛结合到DP 2（View相互作用）DP 2通过荧光技术结合到DP 2（View相互作用）DP 2通过圆二色性结合到DP 2（View相互作用）（C）2010欧洲生物化学学会联合会。Elsevier B. V.出版，保留所有权利。
Archaea-specific D-family DNA polymerase forms a heterotetramer consisting of two large polymerase subunits and two small exonuclease subunits. The N-terminal (1-300) domain structure of the large subunit was determined by X-ray crystallography, although similar to 50 N-terminal residues were disordered. The determined structure consists of nine alpha helices and three beta strands. We also identified the DNA-binding ability of the domain by SPR measurement. The N-terminal (1-100) region plays crucial roles in the folding of the large subunit dimer by connecting the similar to 50 N-terminal residues with their own catalytic region (792-1163).Structured summary:DP2 binds to DP2 by molecular sieving (View interaction)DP2 binds to DP2 by fluorescence technology (View interaction)DP2 binds to DP2 by circular dichroism (View interaction) (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.