PMID:20084272
| Citation |
Holland, PJ and Hollis, T (2010) Structural and mutational analysis of Escherichia coli AlkB provides insight into substrate specificity and DNA damage searching. PLoS ONE 5:e8680 |
|---|---|
| Abstract |
In Escherichia coli, cytotoxic DNA methyl lesions on the N1 position of purines and N3 position of pyrimidines are primarily repaired by the 2-oxoglutarate (2-OG) iron(II) dependent dioxygenase, AlkB. AlkB repairs 1-methyladenine (1-meA) and 3-methylcytosine (3-meC) lesions, but it also repairs 1-methylguanine (1-meG) and 3-methylthymine (3-meT) at a much less efficient rate. How the AlkB enzyme is able to locate and identify methylated bases in ssDNA has remained an open question. |
| Links |
PubMed PMC2800194 Online version:10.1371/journal.pone.0008680 |
| Keywords |
Biocatalysis; Crystallography, X-Ray; DNA Damage; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Mixed Function Oxygenases/chemistry; Mixed Function Oxygenases/genetics; Mixed Function Oxygenases/metabolism; Models, Molecular; Mutagenesis, Site-Directed; Protein Conformation; Substrate Specificity |
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