Structure of the DNA repair helicase XPD

被引：213

作者：

Liu, Huanting ^{[1
]}

Rudolf, Jana ^{[1
]}

Johnson, Kenneth A. ^{[1
]}

McMahon, Stephen A. ^{[1
]}

Oke, Muse ^{[1
]}

Carter, Lester ^{[1
]}

McRobbie, Anne-Marie ^{[1
]}

Brown, Sara E. ^{[1
]}

Naismith, James H. ^{[1
]}

White, Malcolm F. ^{[1
]}

机构：

[1] Univ St Andrews, Ctr Biomol Sci, St Andrews KY16 9ST, Fife, Scotland

来源：

CELL | 2008年 / 133卷 / 05期

基金：

英国生物技术与生命科学研究理事会; 英国医学研究理事会; 英国惠康基金;

关键词：

D O I：

10.1016/j.cell.2008.04.029

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：

The XPD helicase (Rad3 in Saccharomyces cerevisiae) is a component of transcription factor IIH (TFIIH), which functions in transcription initiation and Nucleotide Excision Repair in eukaryotes, catalyzing DNA duplex opening localized to the transcription start site or site of DNA damage, respectively. XPD has a 50 to 30 polarity and the helicase activity is dependent on an iron-sulfur cluster binding domain, a feature that is conserved in related helicases such as FancJ. The xpd gene is the target of mutation in patients with xeroderma pigmentosum, trichothiodystrophy, and Cockayne's syndrome, characterized by a wide spectrum of symptoms ranging from cancer susceptibility to neurological and developmental defects. The 2.25 angstrom crystal structure of XPD from the crenarchaeon Sulfolobus tokodaii, presented here together with detailed biochemical analyses, allows a molecular understanding of the structural basis for helicase activity and explains the phenotypes of xpd mutations in humans.

引用

页码：801 / 812

页数：12

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