Atomic substitution reveals the structural basis for substrate adenine recognition and removal by adenine DNA glycosylase.

ABSTRACT: Adenine DNA glycosylase catalyzes the glycolytic removal of adenine from the promutagenic A.oxoG base pair in DNA. The general features of DNA recognition by an adenine DNA glycosylase, Bacillus stearothermophilus MutY, have previously been revealed via the X-ray structure of a catalytically inactive mutant protein bound to an A:oxoG-containing DNA duplex. Although the structure revealed the substrate adenine to be, as expected, extruded from the DNA helix and inserted into an extrahelical active site pocket on the enzyme, the substrate adenine engaged in no direct contacts with active site residues. This feature was paradoxical, because other glycosylases have been observed to engage their substrates primarily through direct contacts. The lack of direct contacts in the case of MutY sugges

SUBMITTER: Lee S 

PROVIDER: S-EPMC2773975 | biostudies-literature | 2009 Nov

REPOSITORIES: biostudies-literature