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• W1997408199 endingPage "5016" @default.
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• W1997408199 abstract "Escherichia coli endonuclease VIII (Nei) excises oxidized pyrimidines from DNA. It shares significant sequence homology and similar mechanism with Fpg, a bacterial 8-oxoguanine glycosylase. The structure of a covalent Nei–DNA complex has been recently determined, revealing critical amino acid residues which are important for DNA binding and catalysis. Several Fpg structures have also been reported; however, analysis of structural dynamics of Fpg/Nei family proteins has been hindered by the lack of structures of uncomplexed and DNA-bound enzymes from the same source. We report a 2.8 Å resolution structure of free wild-type Nei and two structures of its inactive mutants, Nei-E2A (2.3 Å) and Nei-R252A (2.05 Å). All three structures are virtually identical, demonstrating that the mutations did not affect the overall conformation of the protein in its free state. The structures show a significant conformational change compared with the Nei structure in its complex with DNA, reflecting a ∼50° rotation of the two main domains of the enzyme. Such interdomain flexibility has not been reported previously for any DNA glycosylase and may present the first evidence for a global DNA-induced conformational change in this class of enzymes. Several local but functionally relevant structural changes are also evident in other parts of the enzyme." @default.
• W1997408199 created "2016-06-24" @default.
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• W1997408199 date "2005-09-06" @default.
• W1997408199 modified "2023-09-27" @default.
• W1997408199 title "Structure of the uncomplexed DNA repair enzyme endonuclease VIII indicates significant interdomain flexibility" @default.
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• W1997408199 doi "https://doi.org/10.1093/nar/gki796" @default.
• W1997408199 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1199562" @default.
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