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Very-short-patch repair (Vsr) enzymes occur in a variety of bacteria, where they initiate nucleotide excision repair of G:T mismatches arising by deamination of 5-methyl-cytosines in specific regulatory sequences. We have now determined the structure of the archetypal dcm-Vsr endonuclease from Escherichia coli bound to the cleaved authentic hemi-deaminated/hemi-methylated dcm sequence 5'-C-OH-3' 5'-p-T-p-A-p-G-p-G-3'/3'-G-p-G-p-T-p(Me5)C-p-C formed by self-assembly of a 12mer oligonucleotide into a continuous nicked DNA superhelix. The structure reveals the presence of a Hoogsteen base pair within the deaminated recognition sequence and the substantial distortions of the DNA that accompany Vsr binding to product sites.


Journal article


Nucleic Acids Res

Publication Date





1633 - 1639


Base Pair Mismatch, Base Sequence, Crystallography, X-Ray, DNA Repair, DNA, Bacterial, DNA-Binding Proteins, Endodeoxyribonucleases, Escherichia coli, Models, Molecular, Nucleic Acid Conformation, Oligonucleotides, Protein Binding