AlkA_NAlkA N-terminal domain
|SMART accession number:||SM01009|
|Description:||This domain is found at the N terminus of bacterial AlkA . AlkA (3-methyladenine-DNA 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 flips a 1-azaribose abasic nucleotide out of DNA. This produces a 66 degrees bend in the DNA and a marked widening of the minor groove (PUBMED:10675345).|
|Interpro abstract (IPR010316):|
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 [(PUBMED:8706136)]. The structural analysis of the AlkA and AlkA-hypoxanthine structures indicate that free hypoxanthine binding in the active site may inhibit glycosylase activity [(PUBMED:12009927)].
The AlkA protein consists of three domains: an N-terminal mixed alpha-beta structure, a central seven-helix bundle, and a C-terminal domain of four a helices [(PUBMED:8706136)]. This entry represents the N-terminal domain.
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