title: Structure and specificity of FEN-1 from Methanopyrus kandleri.
abstract: 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.
authors.affiliation: Department of Chemistry and Biochemistry, University of Arizona, Tucson, Arizona, 85721.
authors.forename: Santosh
authors.initials: S
authors.lastname: Shah
authors.forename: Pete
authors.initials: P
authors.lastname: Dunten
authors.forename: Amanda
authors.initials: A
authors.lastname: Stiteler
authors.forename: Chad K
authors.initials: CK
authors.lastname: Park
authors.forename: Nancy C
authors.initials: NC
authors.lastname: Horton
mesh_terms: D000595:Amino Acid Sequence; D019843:Archaeal Proteins / Q000737:chemistry* / Q000378:metabolism*; D018360:Crystallography, X-Ray; D004247:DNA / Q000378:metabolism; D053837:DNA Cleavage; D019605:Euryarchaeota / Q000201:enzymology*; D045585:Flap Endonucleases / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D008969:Molecular Sequence Data; D011485:Protein Binding; D017433:Protein Structure, Secondary; D040681:Structural Homology, Protein; D013379:Substrate Specificity
chemical_list: D019843:Archaeal Proteins; D004247:DNA; D045585:Flap Endonucleases
keywords: DNA nuclease; nucleotide excision repair; protein-DNA complex