Structure and specificity of FEN-1 from Methanopyrus kandleri

Santosh Shah, Pete Dunten, Amanda Stiteler, Chad K. Park, Nancy C. Horton

Research output: Contribution to journalArticlepeer-review


DNA repair is fundamental to genome stability and is found in all three domains of life. However many archaeal species, such as Methanopyrus kandleri, contain only a subset of the eukaryotic nucleotide excision repair (NER) homologs, and those present often contain significant differences compared to their eukaryotic homologs. To clarify the role of the NER XPG-like protein Mk0566 from M. kandleri, its biochemical activity and three-dimensional structure were investigated. Both were found to be more similar to human FEN-1 than human XPG, suggesting a biological role in replication and long-patch base excision repair rather than in NER.

Original languageEnglish (US)
Pages (from-to)188-194
Number of pages7
JournalProteins: Structure, Function and Bioinformatics
Issue number1
StatePublished - Jan 2015


  • DNA nuclease
  • Nucleotide excision repair
  • Protein-DNA complex

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Biology


Dive into the research topics of 'Structure and specificity of FEN-1 from Methanopyrus kandleri'. Together they form a unique fingerprint.

Cite this