Overproduction, crystallization and preliminary crystallographic analysis of a novel human DNA-repair enzyme that recognizes oxidative DNA damage.
DNA glycosylases repair oxidative DNA damage caused by free radicals. Recently, NEIL1, a human homolog of Escherichia coli DNA glycosylase endonuclease VIII, has been identified and shown to exhibit broad substrate specificity for a variety of types of pyrimidine-base damage. An active C-terminal deletion construct of NEIL1 was overexpressed in E. coli and crystallized. The unliganded NEIL1 crystallizes in space group R3, with unit-cell parameters a = b = 132.2, c = 51.1 A. Complete data sets were collected from native, selenomethionyl and iodinated NEIL1 to 2.1, 2.3 and 2.4 angstroms, respectively.
Bandaru
Viswanath
V
Department of Microbiology and Molecular Genetics, The Markey Center for Molecular Genetics, The University of Vermont, Stafford Hall, 95 Carrigan Drive, Burlington, VT 05405-0068, USA.
Cooper
Wendy
W
Wallace
Susan S
SS
Doublié
Sylvie
S
D018360:Crystallography, X-Ray; D004247:DNA / Q000737:chemistry; D004249:DNA Damage; D045647:DNA Glycosylases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D004260:DNA Repair; D043224:Deoxyribonuclease (Pyrimidine Dimer) / Q000737:chemistry; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000201:enzymology; D017353:Gene Deletion; D006801:Humans; D010100:Oxygen / Q000737:chemistry*; D017434:Protein Structure, Tertiary
D004247:DNA; D043224:Deoxyribonuclease (Pyrimidine Dimer); D045647:DNA Glycosylases; C473634:NEIL1 protein, human; D010100:Oxygen