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Science 3 December 2004:
Vol. 306. no. 5702, pp. 1789 - 1793
DOI: 10.1126/science.1101598
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Reports

Crystal Structure of a Photolyase Bound to a CPD-Like DNA Lesion After in Situ Repair

Alexandra Mees,1 Tobias Klar,2 Petra Gnau,2 Ulrich Hennecke,1 Andre P. M. Eker,3 Thomas Carell,1* Lars-Oliver Essen2*

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.

1 Department of Chemistry and Biochemistry, Butenandt-Straße 5-13, Ludwig Maximilians University, D-81377 Munich, Germany.
2 Department of Chemistry, Philipps University, Hans-Meerwein-Straße, D-35032 Marburg, Germany.
3 Department of Cell Biology and Genetics, Medisch Genetisch Centrum, Erasmus University Medical Centre, Post Office Box 1738, 3000 DR Rotterdam, Netherlands.

* To whom correspondence should be addressed. E-mail: essen{at}chemie.uni-marburg.de (L.-O.E.) and thomas.carell{at}cup.uni-muenchen.de (T.C.)

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