Crystal Structure of a Photolyase Bound to a CPD-Like DNA Lesion After in Situ Repair
Alexandra MeesDepartment of Cell Biology and Genetics, Medisch Genetisch Centrum, Erasmus University Medical Centre, Post Office Box 1738, 3000 DR Rotterdam, NetherlandsTobias KlarDepartment of Cell Biology and Genetics, Medisch Genetisch Centrum, Erasmus University Medical Centre, Post Office Box 1738, 3000 DR Rotterdam, NetherlandsPetra GnauDepartment of Cell Biology and Genetics, Medisch Genetisch Centrum, Erasmus University Medical Centre, Post Office Box 1738, 3000 DR Rotterdam, NetherlandsUlrich HenneckeDepartment of Cell Biology and Genetics, Medisch Genetisch Centrum, Erasmus University Medical Centre, Post Office Box 1738, 3000 DR Rotterdam, NetherlandsAndré P. M. EkerDepartment of Cell Biology and Genetics, Medisch Genetisch Centrum, Erasmus University Medical Centre, Post Office Box 1738, 3000 DR Rotterdam, NetherlandsThomas CarellDepartment of Cell Biology and Genetics, Medisch Genetisch Centrum, Erasmus University Medical Centre, Post Office Box 1738, 3000 DR Rotterdam, NetherlandsLars‐Oliver EssenDepartment of Cell Biology and Genetics, Medisch Genetisch Centrum, Erasmus University Medical Centre, Post Office Box 1738, 3000 DR Rotterdam, Netherlands
2004en
ABI
Аннотация
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.
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