Crystal structure of a photolyase bound to a CPD-like DNA lesion after in situ repair

Science. 2004 Dec 3;306(5702):1789-93. doi: 10.1126/science.1101598.


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

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Base Pairing
  • Binding Sites
  • Crystallization
  • Crystallography, X-Ray
  • DNA / chemistry*
  • DNA / metabolism
  • DNA Damage*
  • DNA Repair*
  • DNA, Single-Stranded / chemistry
  • DNA, Single-Stranded / metabolism
  • Deoxyribodipyrimidine Photo-Lyase / chemistry*
  • Deoxyribodipyrimidine Photo-Lyase / metabolism
  • Flavin-Adenine Dinucleotide / metabolism
  • Hydrogen Bonding
  • Nucleic Acid Conformation
  • Protein Conformation
  • Pyrimidine Dimers / chemistry*
  • Pyrimidine Dimers / metabolism
  • Synechococcus / enzymology*
  • Thymine / chemistry


  • DNA, Single-Stranded
  • Pyrimidine Dimers
  • Flavin-Adenine Dinucleotide
  • DNA
  • Deoxyribodipyrimidine Photo-Lyase
  • Thymine

Associated data

  • PDB/1TEZ