Structural highlights
Function
[PHR_SYNP6] Involved in repair of UV radiation-induced DNA damage. Catalyzes the light-dependent monomerization (300-600 nm) of cyclobutyl pyrimidine dimers (in cis-syn configuration), which are formed between adjacent bases on the same DNA strand upon exposure to ultraviolet radiation.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Crystal structure of a photolyase bound to a CPD-like DNA lesion after in situ repair.,Mees A, Klar T, Gnau P, Hennecke U, Eker AP, Carell T, Essen LO Science. 2004 Dec 3;306(5702):1789-93. PMID:15576622[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Mees A, Klar T, Gnau P, Hennecke U, Eker AP, Carell T, Essen LO. Crystal structure of a photolyase bound to a CPD-like DNA lesion after in situ repair. Science. 2004 Dec 3;306(5702):1789-93. PMID:15576622 doi:306/5702/1789
