期刊
EMBO JOURNAL
卷 24, 期 5, 页码 885-894出版社
WILEY
DOI: 10.1038/sj.emboj.7600568
关键词
crystallography; DNA damage; DNA repair; nucleotide excision repair; UvrC
资金
- NIGMS NIH HHS [R01 GM070873, GM070873] Funding Source: Medline
Nucleotide excision repair is a highly conserved DNA repair mechanism present in all kingdoms of life. The incision reaction is a critical step for damage removal and is accomplished by the UvrC protein in eubacteria. No structural information is so far available for the 30 incision reaction. Here we report the crystal structure of the N-terminal catalytic domain of UvrC at 1.5 Angstrom resolution, which catalyzes the 30 incision reaction and shares homology with the catalytic domain of the GIY-YIG family of intron-encoded homing endonucleases. The structure reveals a patch of highly conserved residues surrounding a catalytic magnesium-water cluster, suggesting that the metal binding site is an essential feature of UvrC and all GIY-YIG endonuclease domains. Structural and biochemical data strongly suggest that the N-terminal endonuclease domain of UvrC utilizes a novel one-metal mechanism to cleave the phosphodiester bond.
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