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- W2107060906 abstract "DNA glycosylases safeguard the genome by locating and excising chemically modified bases from DNA. AlkD is a recently discovered bacterial DNA glycosylase that removes positively charged methylpurines from DNA, and was predicted to adopt a protein fold distinct from from those of other DNA repair proteins. The crystal structure of Bacillus cereus AlkD presented here shows that the protein is composed exclusively of helical HEAT-like repeats, which form a solenoid perfectly shaped to accommodate a DNA duplex on the concave surface. Structural analysis of the variant HEAT repeats in AlkD provides a rationale for how this protein scaffolding motif has been modified to bind DNA. We report 7mG excision and DNA binding activities of AlkD mutants, along with a comparison of alkylpurine DNA glycosylase structures. Together, these data provide important insight into the requirements for alkylation repair within DNA and suggest that AlkD utilizes a novel strategy to manipulate DNA in its search for alkylpurine bases." @default.
- W2107060906 created "2016-06-24" @default.
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- W2107060906 date "2008-08-01" @default.
- W2107060906 modified "2023-09-26" @default.
- W2107060906 title "A New Protein Architecture for Processing Alkylation Damaged DNA: The Crystal Structure of DNA Glycosylase AlkD" @default.
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- W2107060906 doi "https://doi.org/10.1016/j.jmb.2008.05.078" @default.
- W2107060906 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3763988" @default.
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