1MUG
G:T/U MISMATCH-SPECIFIC DNA GLYCOSYLASE FROM E.COLI
Summary for 1MUG
| Entry DOI | 10.2210/pdb1mug/pdb |
| Descriptor | PROTEIN (G:T/U SPECIFIC DNA GLYCOSYLASE), SULFATE ION (3 entities in total) |
| Functional Keywords | dna-glycosylase, hydrolase |
| Biological source | Escherichia coli |
| Cellular location | Cytoplasm (Potential): P0A9H1 |
| Total number of polymer chains | 1 |
| Total formula weight | 18888.48 |
| Authors | Barrett, T.E.,Savva, R.,Panayotou, G.,Brown, T.,Barlow, T.,Jiricny, J.,Pearl, L.H. (deposition date: 1998-07-10, release date: 1998-07-15, Last modification date: 2024-02-14) |
| 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 Cited by 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: 9489705DOI: 10.1016/S0092-8674(00)80904-6 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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