Pocketing the difference: structures of uracil excision repair proteins.
The recognition of abnormal DNA structure by proteins is fundamentally different from sequence-specific DNA binding. Recent crystal structures of uracil-DNA glycosylases show a novel uracil-binding pocket that explains the enzyme's selectivity for uracil-containing DNA and provide a structural basis for exploring the catalytic mechanism of amino-glycosylic bond cleavage.
Ellenberger
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Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.
D004247:DNA / Q000737:chemistry; D045647:DNA Glycosylases; D011088:DNA Ligases / Q000378:metabolism*; D004260:DNA Repair / Q000502:physiology; D004268:DNA-Binding Proteins / Q000378:metabolism; D006801:Humans; D009699:N-Glycosyl Hydrolases / Q000737:chemistry / Q000378:metabolism; D014498:Uracil / Q000378:metabolism*; D051981:Uracil-DNA Glycosidase
D004268:DNA-Binding Proteins; D014498:Uracil; D004247:DNA; D045647:DNA Glycosylases; D009699:N-Glycosyl Hydrolases; D051981:Uracil-DNA Glycosidase; D011088:DNA Ligases