Crystal structure of the Escherichia coli dcm very-short-patch DNA repair endonuclease bound to its reaction product-site in a DNA superhelix
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)
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Official URL: http://dx.doi.org/10.1093/nar/gkg273
Description/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.
| Item Type: | Article |
|---|---|
| ISSN: | 0305-1048 (print) |
| Uncontrolled Keywords: | mismatch endonuclease, vsr protein, glycosylase, methylation, uracil, recognition, substrate, sequence, complex, 3,n-4-ethenocytosine |
| Related URLs: | http://www.ncbi.nlm.nih.gov/en...med_docsum http://dx.doi.org/10.1093/nar/gkg273 |
| Subjects: | Q Science > QD Chemistry Q Science > QH Natural history > QH426 Genetics |
| Divisions: | University Structure - Pre August 2011 > School of Chemistry |
| ePrint ID: | 19918 |
| URI: | http://eprints.soton.ac.uk/id/eprint/19918 |
| Deposited On: | 23 Feb 2006 |
| Last Modified: | 02 Mar 2012 11:45 |
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