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Structure of the DNA Repair Helicase XPD

DOI: 10.1016/j.cell.2008.04.029 DOI Help
PMID: 18510925 PMID Help

Authors: Huntang Liu (University of St Andrews) , Jana Rudolf (University of St. Andrews) , Kenneth Johnson (University of St Andrews) , Stephen Mcmahon (University of St Andrews) , Muse Oke (University of St. Andrews) , Lester Carter (University of St. Andrews) , Anne-marrie Mcrobbie (University of St. Andrews) , Sara E. Brown (University of St. Andrews) , Malcolm White (University of St. Andrews) , James. Naismith (University of St Andrews)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Cell , VOL 133 (5) , PAGES 801 - 822

State: Published (Approved)
Published: May 2008

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 5? to 3? 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 Å 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.

Journal Keywords: Archaeal; Cockayne; Crystallography; X-Ray; Iron-Sulfur; Models; Molecular; Mutagenesis; Site-Directed; Protein; Tertiary; Sequence; Amino; Structural; Protein; Sulfolobus; Trichothiodystrophy; Xeroderma; Xeroderma Pigmentosum Group D Protein

Subject Areas: Biology and Bio-materials


Instruments: I03-Macromolecular Crystallography

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