1mug
From Proteopedia
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G:T/U MISMATCH-SPECIFIC DNA GLYCOSYLASE FROM E.COLI
Overview
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.
About this Structure
1MUG is a Single protein structure of sequence from Escherichia coli with SO4 as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of a G:T/U mismatch-specific DNA glycosylase: mismatch recognition by complementary-strand interactions., Barrett TE, Savva R, Panayotou G, Barlow T, Brown T, Jiricny J, Pearl LH, Cell. 1998 Jan 9;92(1):117-29. PMID:9489705
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