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    Crystal structure of the escherichia coli dcm very-short-patch DNA repair endonuclease bound to its reaction product-site in a DNA superhelix

    Bunting KA and Roe SM and Headley A and Brown T and Savva, Renos and Pearl LH (2003) Crystal structure of the escherichia coli dcm very-short-patch DNA repair endonuclease bound to its reaction product-site in a DNA superhelix. Nucleic Acids Research 31 (6), pp. 1633-1639. ISSN 0305-1048.

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    Abstract

    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.

    Metadata

    Item Type: Article
    School: Birkbeck Schools and Departments > School of Science > Biological Sciences
    Research Centre: Innovation Management Research, Birkbeck Centre for
    Depositing User: Sarah Hall
    Date Deposited: 14 May 2019 10:51
    Last Modified: 15 Oct 2019 09:03
    URI: http://eprints.bbk.ac.uk/id/eprint/27521

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