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:Matsui, I
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.
来源:FEBS LETTERS
出版年:2011
卷:585
期:3
页码:452-458
DOI:10.1016/j.febslet.2010.12.040
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.
收录类别:SCOPUS;SCIE
WOS核心被引频次:10
Scopus被引频次:11
资源类型:期刊论文
原文链接:https://www.scopus.com/inward/record.uri?eid=2-s2.0-79551469840&doi=10.1016%2fj.febslet.2010.12.040&partnerID=40&md5=2e58a5f88107f869efb17d09ebadd9ab
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