Structural basis for the excision repair of alkylation-damaged DNA

Article Abstract:

The crystal structure of the monofunctional 3-methyladenine DNA glycosylase II, or AlkA, from Escherichia coli is determined using multiwavelength anomalous diffraction from crystals of seleomethionine-substituted AlkA protein. The structure reveals a large hydrophobic cleft rich in aromatic residues. The pi-donor/acceptor interactions involving the cleft may help AlkA recognize electron-deficient methylated bases. Similarities in fold and active site location between AlkA and the bifunctional glycosylase/lyase endonuclease III suggest that the two have related mechanisms for base excision.

Genetic aspects, Escherichia coli, Glycosylation

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Atomic model of a pyrimidine dimer excision repair enzyme complexed with a DNA substrate: structural basis for damaged DNA recognition

Article Abstract:

T4 endonuclease V, a DNA repair enzyme, recognizes damaged DNA duplexes by structural changes in the duplex bound to the enzyme. There is a sharp twist in the pyrimidine dimers (PD). The twist induces a deformation in the DNA phosphate backbone. The adenine base complementary to the 5'PD is present inside a cavity on the enzyme. The conformation of the bound enzyme also shows changes in the carboxyl terminus, side chains, and Arg-22 and Arg-26.

Observations, Enzymes, Conformational analysis, Enzyme structure-activity relationships

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Recognition of a TG Mismatch: the crystal structure of very short patch repair endonuclease in complex with a DNA duplex

Article Abstract:

Results demonstrate that interaction between DNA and the very short patch repair protein leads to an intercalation of three aromatic amino acid residues to DNA thereby dislocating base pair staking. The data point out to the structural basis for TG mismatch recognition in bacteria.

Japan, Statistical Data Included, Usage, Physiological aspects, DNA damage, Crystallography, DNA binding proteins, Restriction enzymes, DNA, DNA restriction enzymes

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