Three-dimensional structure of a DNA repair enzyme, 3-methyladenine DNA glycosylase II, from Escherichia coli

Article Abstract:

Previous research has been successful in determining the different types of DNA glycosylases. However, the three-dimensional structures of many of these glycosylases have remained unknown. The three-dimensional structure of the DNA repair enzyme, 3-methyladenine DNA glycosylase II, from Escherichia coli is determined at 2.3 A resolution. Results show that the enzyme has three domains and an active site located in a cleft between the two helical domains. These indicate broad substrate specificity and simple N-glycosylase activity within the glycosylase.

DNA repair, Enzymes, Enzyme structure-activity relationships

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Crystal structure of a G:T/U mismatch-specific DNA glycosylase: mismatch recognition by complementary-strand interactions

Article Abstract:

Research was conducted to characterize the crystal structure of the mismatch-specific uracil DNA-glycosylase (MUG) enzyme of Escherichia coli alone and in combination with a DNA duplex encoding an abasic reaction product. Polymerase chain reaction was coupled with chromosomal DNA to amplify the coding sequence for Escherichia coli MUG. Oligonucleotides were also determined on a DNA synthesizer via cyanoethyl phosphoramidite chemistry.

DNA, Glycosylation, Complementation (Genetics)

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Insights into multistep phosphorelay from the crystal structure of the C-terminal HPt domain of ArcB

Article Abstract:

Analysis of the three-dimensional structure of the C-terminal histidine-containing phosphotransfer (HPt) domain of ArcB indicated the presence of a kidney-shaped domain with an all-alpha structure. The domain is composed of six helices composed of a pair of long antiparallel helices with a closely packed core. Furthermore, the six alpha helices exhibited four-helix bundle-folding that is common in both eukaryotes and prokaryotes.

Analysis, Proteins, Protein structure, Histidine, Amino acid sequence, Amino acid sequencing

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