CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.10 | Orthogonal Bundle |
|
1.10.1670 | Endonuclease Iii, domain 2 |
|
1.10.1670.10 | Helix-hairpin-Helix base-excision DNA repair enzymes (C-terminal) |
Domain Context
CATH Clusters
| Superfamily | Helix-hairpin-Helix base-excision DNA repair enzymes (C-terminal) |
| Functional Family | Adenine DNA glycosylase |
Enzyme Information
| 3.2.2.31 |
Adenine glycosylase.
based on mapping to UniProt P17802
Hydrolyzes free adenine bases from 7,8-dihydro-8-oxoguanine:adenine mismatched double-stranded DNA, leaving an apurinic site.
-!- The enzyme serves as a mismatch repair enzyme that works to correct 7,8-dihydro-8-oxoguanine:adenine mispairs that arise in DNA when error-prone synthesis occurs past 7,8-dihydro-8-oxoguanine (GO) lesions in DNA. -!- The enzyme excises the adenine of the mispair, producing an apurinic site sensitive to AP endonuclease activity. -!- After removing the undamaged adenine the enzyme remains bound to the site to prevent EC 3.2.2.23 (MutM) from removing the GO lesion, which could lead to a double strand break. -!- In vitro the enzyme is also active with adenine:guanine, adenine:cytosine, and adenine:7,8-dihydro-8-oxoadenine (AO) mispairs, removing the adenine in all cases.
|
UniProtKB Entries (1)
| P17802 |
MUTY_ECOLI
Escherichia coli K-12
Adenine DNA glycosylase
|
PDB Structure
| PDB | 1KQJ |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Noncysteinyl coordination to the [4Fe-4S]2+ cluster of the DNA repair adenine glycosylase MutY introduced via site-directed mutagenesis. Structural characterization of an unusual histidinyl-coordinated cluster.
Biochemistry
|
