Summary information and primary citation
- PDB-id
-
1f4r;
DSSR-derived features in text and
JSON formats; DNAproDB
- Class
- hydrolase-DNA
- Method
- X-ray (2.4 Å)
- Summary
- Crystal structure of the human aag DNA repair
glycosylase complexed with 1,n6-ethenoadenine-DNA
- Reference
-
Lau AY, Wyatt MD, Glassner BJ, Samson LD, Ellenberger T
(2000): "Molecular
basis for discriminating between normal and damaged bases
by the human alkyladenine glycosylase, AAG."
Proc.Natl.Acad.Sci.USA, 97,
13573-13578. doi: 10.1073/pnas.97.25.13573.
- Abstract
- The human 3-methyladenine DNA glycosylase [alkyladenine
DNA glycosylase (AAG)] catalyzes the first step of base
excision repair by cleaving damaged bases from DNA. Unlike
other DNA glycosylases that are specific for a particular
type of damaged base, AAG excises a chemically diverse
selection of substrate bases damaged by alkylation or
deamination. The 2.1-A crystal structure of AAG complexed
to DNA containing 1,N(6)-ethenoadenine suggests how
modified bases can be distinguished from normal DNA bases
in the enzyme active site. Mutational analyses of residues
contacting the alkylated base in the crystal structures
suggest that the shape of the damaged base, its
hydrogen-bonding characteristics, and its aromaticity all
contribute to the selective recognition of damage by
AAG.
