Abstract
DNA photolyases use light energy to repair DNA that comprises ultraviolet-induced lesions such as the cis-syn cyclobutane pyrimidine dimers (CPDs). Here we report the crystal structure of a DNA photolyase bound to duplex DNA that is bent by 50 degrees and comprises a synthetic CPD lesion. This CPD lesion is flipped into the active site and split there into two thymines by synchrotron radiation at 100 K. Although photolyases catalyze blue light-driven CPD cleavage only above 200 K, this structure apparently mimics a structural substate during light-driven DNA repair in which back-flipping of the thymines into duplex DNA has not yet taken place.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Base Pairing
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Binding Sites
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Crystallization
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Crystallography, X-Ray
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DNA / chemistry*
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DNA / metabolism
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DNA Damage*
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DNA Repair*
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DNA, Single-Stranded / chemistry
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DNA, Single-Stranded / metabolism
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Deoxyribodipyrimidine Photo-Lyase / chemistry*
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Deoxyribodipyrimidine Photo-Lyase / metabolism
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Flavin-Adenine Dinucleotide / metabolism
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Hydrogen Bonding
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Nucleic Acid Conformation
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Protein Conformation
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Pyrimidine Dimers / chemistry*
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Pyrimidine Dimers / metabolism
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Synechococcus / enzymology*
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Thymine / chemistry
Substances
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DNA, Single-Stranded
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Pyrimidine Dimers
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Flavin-Adenine Dinucleotide
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DNA
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Deoxyribodipyrimidine Photo-Lyase
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Thymine