Structure of S. tokodaii Xpd4Structure of S. tokodaii Xpd4

Structural highlights

2vl7 is a 1 chain structure with sequence from Sulfurisphaera tokodaii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.25Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Evolutionary Conservation

 

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

Structure of the DNA repair helicase XPD.,Liu H, Rudolf J, Johnson KA, McMahon SA, Oke M, Carter L, McRobbie AM, Brown SE, Naismith JH, White MF Cell. 2008 May 30;133(5):801-12. PMID:18510925[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Liu H, Rudolf J, Johnson KA, McMahon SA, Oke M, Carter L, McRobbie AM, Brown SE, Naismith JH, White MF. Structure of the DNA repair helicase XPD. Cell. 2008 May 30;133(5):801-12. PMID:18510925 doi:10.1016/j.cell.2008.04.029

2vl7, resolution 2.25Å

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