1ODG

Very-short-patch DNA repair endonuclease bound to its reaction product site

Summary for 1ODG

• Entry DOI: 10.2210/pdb1odg/pdb
• Related: 1CW0 1VSR
• Descriptor: DNA MISMATCH ENDONUCLEASE, 5'-D(*TP*AP*GP*GP*CP*5CM*TP*GP*GP*AP*TP*CP)-3', ZINC ION, ... (4 entities in total)
• Functional Keywords: hydrolase, dna repair, endonuclease, very short patch repair, dna repai hydrolase, nuclease, zinc, metal-binding
• Biological source: ESCHERICHIA COLI; More
• Total number of polymer chains: 3
• Total formula weight: 23019.09

Authors

Bunting, K.A.,Roe, S.M.,Headley, A.,Brown, T.,Savva, R.,Pearl, L.H. (deposition date: 2003-02-19, release date: 2003-03-13, Last modification date: 2023-12-13)

Primary citation

Bunting, K.A.,Roe, S.M.,Headley, A.,Brown, T.,Savva, R.,Pearl, L.H.
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 Res., 31:1633-, 2003

PubMed 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.

PubMed: 12626704
DOI: 10.1093/NAR/GKG273

Experimental method

X-RAY DIFFRACTION (2.8 Å)