PMID:12009927
| Citation |
Teale, M, Symersky, J and DeLucas, L 3-methyladenine-DNA glycosylase II: the crystal structure of an AlkA-hypoxanthine complex suggests the possibility of product inhibition. Bioconjug. Chem. 13:403-7 |
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| Abstract |
Escherichia coli (E. coli) protein 3-methyladenine-DNA glycosylase II (AlkA) functions primarily by removing alkylation damage from duplex and single stranded DNA. A crystal structure of AlkA was refined to 2.0 A resolution. This structure in turn was used to refine an AlkA-hypoxanthine (substrate) complex structure to 2.4 A resolution. The complex structure shows hypoxanthine located in AlkA's active site stacked between residues W218 and Y239. The structural analysis of the AlkA and AlkA-hypoxanthine structures indicate that free hypoxanthine binding in the active site may inhibit glycosylase activity. |
| Links | |
| Keywords |
Crystallization; DNA Glycosylases; Enzyme Inhibitors/pharmacology; Escherichia coli/enzymology; Escherichia coli/genetics; Hypoxanthines/chemistry; Models, Molecular; N-Glycosyl Hydrolases/antagonists & inhibitors; N-Glycosyl Hydrolases/chemistry; N-Glycosyl Hydrolases/metabolism; Tryptophan/chemistry; Tyrosine/chemistry; X-Ray Diffraction |
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