期刊
EMBO JOURNAL
卷 26, 期 2, 页码 613-622出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/sj.emboj.7601497
关键词
DNA damage; DNA repair; endonuclease; nucleotide excision repair; UvrC; RNase H
资金
- Intramural NIH HHS Funding Source: Medline
- NIGMS NIH HHS [GM070873, R01 GM070873] Funding Source: Medline
Removal and repair of DNA damage by the nucleotide excision repair pathway requires two sequential incision reactions, which are achieved by the endonuclease UvrC in eubacteria. Here, we describe the crystal structure of the C-terminal half of UvrC, which contains the catalytic domain responsible for 50 incision and a helix-hairpin helix-domain that is implicated in DNA binding. Surprisingly, the 50 catalytic domain shares structural homology with RNase H despite the lack of sequence homology and contains an uncommon DDH triad. The structure also reveals two highly conserved patches on the surface of the protein, which are not related to the active site. Mutations of residues in one of these patches led to the inability of the enzyme to bind DNA and severely compromised both incision reactions. Based on our results, we suggest a model of how UvrC forms a productive protein-DNA complex to excise the damage from DNA.
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