IPR037046
DNA-3-methyladenine glycosylase AlkA, N-terminal domain superfamily
InterPro entry
Short name | AlkA_N_sf |
Overlapping entries |
Description
AlkA (DNA-3-methyladenine glycosylase II) is a base excision repair glycosylase from Escherichia coli. It removes a variety of alkylated bases from DNA, primarily by removing alkylation damage from duplex and single stranded DNA. AlkA is similar in fold and active site location to the bifunctional glycosylase/lyase endonuclease III. This suggests that the two may use similar mechanisms for base excision
[1]. The structural analysis of the AlkA and AlkA-hypoxanthine structures indicate that free hypoxanthine binding in the active site may inhibit glycosylase activity
[2].
The AlkA protein consists of three domains: an N-terminal mixed α-β structure, a central seven-helix bundle, and a C-terminal domain of four a helices
[1]. This entry represents the N-terminal domain superfamily.
References
1.Structural basis for the excision repair of alkylation-damaged DNA. Labahn J, Scharer OD, Long A, Ezaz-Nikpay K, Verdine GL, Ellenberger TE. Cell 86, 321-9, (1996). View articlePMID: 8706136
2.3-methyladenine-DNA glycosylase II: the crystal structure of an AlkA-hypoxanthine complex suggests the possibility of product inhibition. Teale M, Symersky J, DeLucas L. Bioconjug. Chem. 13, 403-7, (2002). View articlePMID: 12009927
Cross References
ENZYME
Contributing Member Database Entry
- CATH-Gene3D:G3DSA:3.30.310.20