Abstract
Escherichia coli UvrD protein is a superfamily 1 DNA helicase which plays a crucial role in nucleotide excision repair and methyl-directed mismatch repair. There is a general consensus that the enzyme unwinds a duplex DNA from a 3′ end single-stranded DNA (ssDNA) tail, a gap or a nick. However, conflicting models for the unwinding mechanism have been proposed. Concerning its stoichiometry, some biochemical studies have suggested that the enzyme has optimal activity as an oligomeric form. However, a structural study has indicated that the enzyme functions as a monomer deduced from structural analysis of UvrD-DNA complexes.
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