Crystal structure of a G:T/U mismatch-specific DNA glycosylase: mismatch recognition by complementary-strand interactions
| Autor: | T E, Barrett, R, Savva, G, Panayotou, T, Barlow, T, Brown, J, Jiricny, L H, Pearl |
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| Rok vydání: | 1998 |
| Předmět: |
DNA
Complementary Endodeoxyribonucleases DNA Repair Sequence Homology Amino Acid Molecular Sequence Data Nucleic Acid Heteroduplexes DNA Crystallography X-Ray Catalysis DNA Glycosylases Substrate Specificity Deoxyribonuclease (Pyrimidine Dimer) Viral Proteins Escherichia coli Amino Acid Sequence Crystallization Uracil-DNA Glycosidase N-Glycosyl Hydrolases DNA Damage Protein Binding |
| Zdroj: | Cell. 92(1) |
| ISSN: | 0092-8674 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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