DNA-bound structures and mutants reveal absasic DNA binding by APE1 DNA repair and coordination
Article Abstract:
Three co-crystal structures of human APE1 bound to abasic DNA are reported. These show that APE1 uses a rigid, pre-formed and positively charged surface to bend the DNA helix and incorporate the AP-DNA strand. Human APE1 is shown to be structurally optimized to retain cleaved DNA, and it may displace bound glycosylases, retaining the nicked DNA product.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2000
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Structure and function of the multifunctional DNA-repair enzyme exonuclease III
Article Abstract:
A2-fold symmetric, four layered alpha-beta fold with similarities to the RNase H and deoxyribonuclease I is exhibited by the crystal structure of the exonuclease III. The dCMP and Mn doubly ionized ions are bound to the exonuclease III at the end of the alpha beta-sandwich. The binding occurs in the region which is dominated by the positive electrostatic potential.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1995
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A nucleotide-flipping mechanism from the structure of human uracil-DNA glycosylase bound to DNA
Article Abstract:
The base-excision DNA-repair enzyme, uracil-DNA glycosylase (UDG) binding with damaged DNA involves a nucleotide-flipping mechanism. The electrostatic orientation of the UDG site along the target DNA, compression of the DNA backbone and the insertion of an amino acid into the DNA are responsible for the flipping out of the damaged DNA base from the major groove. This nucleotide flipping helps in the recognition of the phosphate, deoxyribose and uracil bases of the DNA major groove.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1996
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