1MUG

G:T/U MISMATCH-SPECIFIC DNA GLYCOSYLASE FROM E.COLI

1MUG の概要

• エントリーDOI: 10.2210/pdb1mug/pdb
• 分子名称: PROTEIN (G:T/U SPECIFIC DNA GLYCOSYLASE), SULFATE ION (3 entities in total)
• 機能のキーワード: dna-glycosylase, hydrolase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm (Potential): P0A9H1
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18888.48

構造登録者

Barrett, T.E.,Savva, R.,Panayotou, G.,Brown, T.,Barlow, T.,Jiricny, J.,Pearl, L.H. (登録日: 1998-07-10, 公開日: 1998-07-15, 最終更新日: 2024-02-14)

主引用文献

Barrett, T.E.,Savva, R.,Panayotou, G.,Barlow, T.,Brown, T.,Jiricny, J.,Pearl, L.H.
Crystal structure of a G:T/U mismatch-specific DNA glycosylase: mismatch recognition by complementary-strand interactions.
Cell(Cambridge,Mass.), 92:117-129, 1998

PubMed 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.

PubMed: 9489705
DOI: 10.1016/S0092-8674(00)80904-6

実験手法

X-RAY DIFFRACTION (1.8 Å)