2VL7

Structure of S. tokodaii Xpd4

Summary for 2VL7

• Entry DOI: 10.2210/pdb2vl7/pdb
• Descriptor: XPD, PHOSPHATE ION (3 entities in total)
• Functional Keywords: helicase, unknown function
• Biological source: SULFOLOBUS TOKODAII
• Total number of polymer chains: 1
• Total formula weight: 62421.45

Authors

Naismith, J.H.,Johnson, K.A.,Oke, M.,McMahon, S.A.,Liu, L.,White, M.F.,Zawadski, M.,Carter, L.G. (deposition date: 2008-01-08, release date: 2008-05-13, Last modification date: 2024-11-20)

Primary citation

Liu, L.,Johnson, K.A.,Rudolf, J.,Mcrobbie, A.-M.,Mcmahon, S.A.,Oke, M.,Carter, L.G.,Naismith, J.H.,White, M.F.
Structure of the DNA Repair Helicase Xpd.
Cell(Cambridge,Mass.), 133:801-, 2008

PubMed 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 A 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.

PubMed: 18510925
DOI: 10.1016/J.CELL.2008.04.029

Experimental method

X-RAY DIFFRACTION (2.25 Å)