1MWI

Crystal structure of a MUG-DNA product complex

Summary for 1MWI

• Entry DOI: 10.2210/pdb1mwi/pdb
• Related: 1MUG
• Descriptor: 5'-D(*CP*GP*CP*GP*AP*GP*(AAB)P*TP*CP*GP*CP*G)-3', G/U mismatch-specific DNA glycosylase (3 entities in total)
• Functional Keywords: dna-glycosylase, nucleotide flipping, abasic site, hydrolase-dna complex, hydrolase/dna
• Biological source: Escherichia coli
• Cellular location: Cytoplasm (Potential): P0A9H1
• Total number of polymer chains: 2
• Total formula weight: 22267.65

Authors

Barrett, T.E.,Savva, R.,Panayotou, G.,Brown, T.,Barlow, T.,Jiricny, J.,Pearl, L.H. (deposition date: 2002-09-30, release date: 2002-10-04, Last modification date: 2024-04-03)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.35 Å)