Crystal Structure of a Photolyase Bound to a CPD-Like DNA Lesion After in Situ Repair
- 3 December 2004
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 306 (5702) , 1789-1793
- https://doi.org/10.1126/science.1101598
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° 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.Keywords
This publication has 25 references indexed in Scilit:
- Structure and Function of DNA Photolyase and Cryptochrome Blue-Light PhotoreceptorsChemical Reviews, 2003
- Cyclobutylpyrimidine Dimer Base Flipping by DNA PhotolyaseJournal of Biological Chemistry, 2002
- UV-induced DNA damage and repair: a reviewPhotochemical & Photobiological Sciences, 2002
- Crystal structure of thermostable DNA photolyase: Pyrimidine-dimer recognition mechanismProceedings of the National Academy of Sciences, 2001
- The mechanism of action of DNA photolyasesCurrent Opinion in Chemical Biology, 2001
- Theoretical Study of Electron Transfer between the Photolyase Catalytic Cofactor FADH- and DNA Thymine DimerJournal of the American Chemical Society, 2000
- A Model for the Enzyme−Substrate Complex of DNA Photolyase and Photodamaged DNAJournal of the American Chemical Society, 1999
- Evidence for Dinucleotide Flipping by DNA PhotolyaseJournal of Biological Chemistry, 1998
- Crystal structure of DMA photolyase from Anacystis nidulansNature Structural & Molecular Biology, 1997
- Crystal Structure of DNA Photolyase from Escherichia coliScience, 1995