PMID:9489705
| Citation |
Barrett, TE, Savva, R, Panayotou, G, Barlow, T, Brown, T, Jiricny, J and Pearl, LH (1998) Crystal structure of a G:T/U mismatch-specific DNA glycosylase: mismatch recognition by complementary-strand interactions. Cell 92:117-29 |
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| Abstract |
G:U mismatches resulting from deamination of cytosine are the most common promutagenic lesions occurring in DNA. Uracil is removed in a base-excision repair pathway by uracil DNA-glycosylase (UDG), which excises uracil from both single- and double-stranded DNA. Recently, a biochemically distinct family of DNA repair enzymes has been identified, which excises both uracil and thymine, but only from mispairs with guanine. Crystal structures of the mismatch-specific uracil DNA-glycosylase (MUG) from E. coli, and of a DNA complex, reveal a remarkable structural and functional homology to UDGs despite low sequence identity. Details of the MUG structure explain its thymine DNA-glycosylase activity and the specificity for G:U/T mispairs, which derives from direct recognition of guanine on the complementary strand. |
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| Keywords |
Amino Acid Sequence; Catalysis; Crystallization; Crystallography, X-Ray; DNA/chemistry; DNA/metabolism; DNA Damage; DNA Glycosylases; DNA Repair; DNA, Complementary/chemistry; DNA, Complementary/metabolism; Deoxyribonuclease (Pyrimidine Dimer); Endodeoxyribonucleases/chemistry; Endodeoxyribonucleases/metabolism; Escherichia coli/chemistry; Escherichia coli/enzymology; Molecular Sequence Data; N-Glycosyl Hydrolases/antagonists & inhibitors; N-Glycosyl Hydrolases/chemistry; N-Glycosyl Hydrolases/metabolism; Nucleic Acid Heteroduplexes/chemistry; Protein Binding; Sequence Homology, Amino Acid; Substrate Specificity; Uracil-DNA Glycosidase; Viral Proteins/pharmacology |
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