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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

Crystal structure of the Escherichia coli dcm very-short-patch DNA repair endonuclease bound to its reaction product-site in a DNA superhelix
Crystal structure of the Escherichia coli dcm very-short-patch DNA repair endonuclease bound to its reaction product-site in a DNA superhelix
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-pMe5C-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.
mismatch endonuclease, vsr protein, glycosylase, methylation, uracil, recognition, substrate, sequence, complex, 3, n-4-ethenocytosine
0305-1048
1633-1639
Bunting, Karen A.
7faf21b6-ef31-429e-a05a-43cafeb87a46
Roe, S. Mark
e79cf104-6593-43e1-b5b0-2991127f6bad
Headley, Anthony
5b81543e-c8c0-4401-958b-6f14d622963a
Brown, Tom
a64aae36-bb30-42df-88a2-11be394e8c89
Savva, Renos
41978193-487f-438f-899d-40d969691104
Pearl, Laurence H.
ac0a1708-ac16-4b7d-a0f5-8354956b2cc0
Bunting, Karen A.
7faf21b6-ef31-429e-a05a-43cafeb87a46
Roe, S. Mark
e79cf104-6593-43e1-b5b0-2991127f6bad
Headley, Anthony
5b81543e-c8c0-4401-958b-6f14d622963a
Brown, Tom
a64aae36-bb30-42df-88a2-11be394e8c89
Savva, Renos
41978193-487f-438f-899d-40d969691104
Pearl, Laurence H.
ac0a1708-ac16-4b7d-a0f5-8354956b2cc0

Bunting, Karen A., Roe, S. Mark, Headley, Anthony, Brown, Tom, Savva, Renos and Pearl, Laurence H. (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), 1633-1639. (doi:10.1093/nar/gkg273).

Record type: Article

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-pMe5C-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.

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More information

Published date: 15 March 2003
Keywords: mismatch endonuclease, vsr protein, glycosylase, methylation, uracil, recognition, substrate, sequence, complex, 3, n-4-ethenocytosine

Identifiers

Local EPrints ID: 19918
URI: https://eprints.soton.ac.uk/id/eprint/19918
ISSN: 0305-1048
PURE UUID: ec0f3dd1-973a-4018-aac3-1c2910cc3cdd

Catalogue record

Date deposited: 23 Feb 2006
Last modified: 17 Jul 2017 16:30

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