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. 1995 Mar 24;80(6):869-78.
doi: 10.1016/0092-8674(95)90290-2.

Crystal structure and mutational analysis of human uracil-DNA glycosylase: structural basis for specificity and catalysis

C D Mol  1 , A S Arvai, G Slupphaug, B Kavli, I Alseth, H E Krokan, J A Tainer
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Free article

Crystal structure and mutational analysis of human uracil-DNA glycosylase: structural basis for specificity and catalysis

C D Mol et al. Cell. .
Free article

Abstract

Crystal structures of the DNA repair enzyme human uracil-DNA glycosylase (UDG), combined with mutational analysis, reveal the structural basis for the specificity of the enzyme. Within the classic alpha/beta fold of UDG, sequence-conserved residues form a positively charged, active-site groove the width of duplex DNA, at the C-terminal edge of the central four-stranded parallel beta sheet. In the UDG-6-aminouracil complex, uracil binds at the base of the groove within a rigid preformed pocket that confers selectivity for uracil over other bases by shape complementary and by main chain and Asn-204 side chain hydrogen bonds. Main chain nitrogen atoms are positioned to stabilize the oxyanion intermediate generated by His-268 acting via nucleophilic attack or general base mechanisms. Specific binding of uracil flipped out from a DNA duplex provides a structural mechanism for damaged base recognition.

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