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Structure of the DNA repair helicase XPD

Research output: Contribution to journalArticlepeer-review

Author(s)

Huanting Liu, Jana Rudolf, K A Johnson, Stephen McMahon, Muse Oke, L Carter, A-M McRobbie, S E Brown, James Henderson Naismith, Malcolm Frederick White

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Abstract

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.

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Details

Original languageEnglish
Pages (from-to)801-812
Number of pages12
JournalCell
Volume133
Issue number5
DOIs
Publication statusPublished - 30 May 2008

    Research areas

  • XERODERMA-PIGMENTOSUM, CRYSTAL-STRUCTURE, COCKAYNE-SYNDROME, BASAL TRANSCRIPTION, DIFFRACTION DATA, TRICHOTHIODYSTROPHY, DEFICIENT, MUTATIONS, SEQUENCE, FEATURES

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