1mug: Difference between revisions
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'''G:T/U MISMATCH-SPECIFIC DNA GLYCOSYLASE FROM E.COLI''' | '''G:T/U MISMATCH-SPECIFIC DNA GLYCOSYLASE FROM E.COLI''' | ||
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[[Category: Pearl, L H.]] | [[Category: Pearl, L H.]] | ||
[[Category: Savva, R.]] | [[Category: Savva, R.]] | ||
[[Category: | [[Category: Dna-glycosylase]] | ||
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Revision as of 22:43, 2 May 2008
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. 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 Page seeded by OCA on Sat May 3 01:43:46 2008
