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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.

Type

Journal article

Journal

Nucleic Acids Res

Publication Date

15/03/2003

Volume

31

Pages

1633 - 1639

Keywords

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