Evidence map›Paper›PMID 18578568›Full record

ArticlePLoS biology2008

Crystal structure of the FeS cluster-containing nucleotide excision repair helicase XPD.

Stefanie C Wolski, Jochen Kuper, Petra Hänzelmann, James J Truglio, Deborah L Croteau, Bennett Van Houten, Caroline Kisker

Open access · goldAbstract read
In one paragraph

Article in PLoS biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 128 papers.

0numbers the graph read from it
0cells of the map it votes in
128citing papers in PubMed
6.3field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

128 citing papers in PubMed, 213 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. A new crystal form of the DNA-free full-length XPD helicase from Thermoplasma acidophilum.Acta crystallographica. Section F, Structural biology communications · 2026
    Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Structure, function and evolution of the bacterial DinG-like proteins.Computational and structural biotechnology journal · 2025
    Review
  12. The Role of SF1 and SF2 Helicases in Biotechnological Applications.Applied biochemistry and biotechnology · 2024
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Mechanism of action of nucleotide excision repair machinery.Biochemical Society transactions · 2022
    Review
  20. Review

68 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 4 institutions in 2 countries.

Stefanie C WolskiRudolf Virchow Center for Experimental Biomedicine, Institute for Structural Biology, University of Würzburg, Würzburg, Germany.
Jochen Kuper
Petra Hänzelmann
James J Truglio
Deborah L Croteau
Bennett Van Houten
Caroline Kisker
University of Würzburg · DENational Institute of Environmental Health Sciences · USNational Institutes of Health · USStony Brook University · US

Funding

Studies Of Nucleotide Excision Repair ProteinsZ01ES061060 · NIEHS · NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES · PI VAN HOUTEN, BENNETT · 1999 to 2008
$1.9M
Intramural NIH HHSMedical Research Council G0500367
6 · The paper itself

Abstract

DNA damage recognition by the nucleotide excision repair pathway requires an initial step identifying helical distortions in the DNA and a proofreading step verifying the presence of a lesion. This proofreading step is accomplished in eukaryotes by the TFIIH complex. The critical damage recognition component of TFIIH is the XPD protein, a DNA helicase that unwinds DNA and identifies the damage. Here, we describe the crystal structure of an archaeal XPD protein with high sequence identity to the human XPD protein that reveals how the structural helicase framework is combined with additional elements for strand separation and DNA scanning. Two RecA-like helicase domains are complemented by a 4Fe4S cluster domain, which has been implicated in damage recognition, and an alpha-helical domain. The first helicase domain together with the helical and 4Fe4S-cluster-containing domains form a central hole with a diameter sufficient in size to allow passage of a single stranded DNA. Based on our results, we suggest a model of how DNA is bound to the XPD protein, and can rationalize several of the mutations in the human XPD gene that lead to one of three severe diseases, xeroderma pigmentosum, Cockayne syndrome, and trichothiodystrophy.

Indexed as

Amino Acid SequenceAnimalsArchaeal ProteinsBase SequenceCrystallography, X-RayDNA PrimersDNA RepairHumansIron-Sulfur ProteinsModels, MolecularMolecular Sequence DataProtein ConformationSequence Homology, Amino AcidStatic ElectricityXeroderma Pigmentosum Group D ProteinArchaeal ProteinsDNA PrimersERCC2 protein, humanIron-Sulfur ProteinsXeroderma Pigmentosum Group D Protein

Identifiers

PMID18578568
PMCPMC2435149
OpenAlexW2064853448

What OpenQuestion holds

Textmetadata
LicenceCC0
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.