What More is Learned from a Crystal Structure of Escherichia coli Uracil DNA Glycosylase at 0.94 Å?
Gaoyi Xiao, Maria Tordova, James T. Stivers, and Gary L. Gilliland, Center for Advanced Research in Biotechnology, University of Maryland Biotechnology Institute and the National Institute for Standards and Technology, 9600 Gudelsky Drive Rockville, MD 20850 The DNA repair enzyme uracil DNA glycosylase (UDG) catalyzes the hydrolysis of premutagenic uracil (U) residues from single-stranded or duplex DNA, producing free U and abasic DNA (AB-DNA). We report here the crystal structure of uracil DNA glycosylase (UDG) from Escherichia coli strain B, which represents the first structure of a prokaryotic UDG. The protein was crystallized from PEG4000 in space group P212121 with cell parameters a=54.85, b=58.93 and c=63.99 Å. The highest resolution data (0.94 Å) was collected under cryogenic condition at the Advanced Photon Source. The structure was solved using combined techniques of single isomorphous replacement with anomalous scattering with PHASES (Furrey, 1994) and molecular replacement w
