标题：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
作者：Matsui, Ikuo; Urushibata, Yuji; Shen, Yulong; Matsui, Eriko; Yokoyama, Hideshi
作者机构：[Matsui, Ikuo; Urushibata, Yuji; Shen, Yulong; Matsui, Eriko] Natl Inst Adv Ind Sci & Technol, Biomed Res Inst, Tsukuba, Ibaraki 3058566, Japan.; [S 更多
通讯作者地址：[Matsui, I]Natl Inst Adv Ind Sci & Technol, Biomed Res Inst, 1-1-1 Higashi, Tsukuba, Ibaraki 3058566, Japan.
关键词：D-family DNA polymerase; DNA replication; Binding domain; Molecular; structure; Hyperthermophilic archaea; Pyrococcus
摘要：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.