Structure of the DNA repair helicase XPD

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

doi:10.1016/j.cell.2008.04.029

Structure of the DNA repair helicase XPD

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

Research output: Contribution to journal › Article › peer-review

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.

Original language	English
Pages (from-to)	801-812
Number of pages	12
Journal	Cell
Volume	133
Issue number	5
DOIs	https://doi.org/10.1016/j.cell.2008.04.029
Publication status	Published - 30 May 2008

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

Keywords

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

Access to Document

10.1016/j.cell.2008.04.029

Cite this

@article{72baff1d246d4befbeead16b299a6edb,

title = "Structure of the DNA repair helicase XPD",

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.",

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

author = "Huanting Liu and Jana Rudolf and Johnson, \{K A\} and Stephen McMahon and Muse Oke and L Carter and A-M McRobbie and Brown, \{S E\} and Naismith, \{James Henderson\} and White, \{Malcolm Frederick\}",

year = "2008",

month = may,

day = "30",

doi = "10.1016/j.cell.2008.04.029",

language = "English",

volume = "133",

pages = "801--812",

journal = "Cell",

issn = "0092-8674",

publisher = "Elsevier",

number = "5",

}

TY - JOUR

T1 - Structure of the DNA repair helicase XPD

AU - Liu, Huanting

AU - Rudolf, Jana

AU - Johnson, K A

AU - McMahon, Stephen

AU - Oke, Muse

AU - Carter, L

AU - McRobbie, A-M

AU - Brown, S E

AU - Naismith, James Henderson

AU - White, Malcolm Frederick

PY - 2008/5/30

Y1 - 2008/5/30

N2 - 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.

AB - 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.

KW - XERODERMA-PIGMENTOSUM

KW - CRYSTAL-STRUCTURE

KW - COCKAYNE-SYNDROME

KW - BASAL TRANSCRIPTION

KW - DIFFRACTION DATA

KW - TRICHOTHIODYSTROPHY

KW - DEFICIENT

KW - MUTATIONS

KW - SEQUENCE

KW - FEATURES

UR - https://www.scopus.com/pages/publications/43949110271

U2 - 10.1016/j.cell.2008.04.029

DO - 10.1016/j.cell.2008.04.029

M3 - Article

SN - 0092-8674

VL - 133

SP - 801

EP - 812

JO - Cell

JF - Cell

IS - 5

ER -

Structure of the DNA repair helicase XPD

Abstract

UN SDGs

Keywords

Access to Document

Other files and links

Fingerprint

BBSRC BBS/B/14426: SPORT

Cite this

Structure of the DNA repair helicase XPD

Abstract

UN SDGs

Keywords

Access to Document

Other files and links

Fingerprint

Projects

BBSRC BBS/B/14426: SPORT

Cite this