1TEZ
COMPLEX BETWEEN DNA AND THE DNA PHOTOLYASE FROM ANACYSTIS NIDULANS
Summary for 1TEZ
Entry DOI | 10.2210/pdb1tez/pdb |
Descriptor | 5'-D(*AP*TP*CP*GP*GP*CP*T*(TCP)P*CP*GP*C)-3', 5'-D(P*CP*GP*AP*AP*GP*CP*CP*GP*A)-3', 5'-D(*TP*CP*GP*C)-3', ... (9 entities in total) |
Functional Keywords | photolyase; dna repair; light-driven electron transfer, lyase-dna complex, lyase/dna |
Biological source | Synechococcus elongatus PCC 6301 More |
Total number of polymer chains | 12 |
Total formula weight | 235903.52 |
Authors | Essen, L.-O.,Carell, T.,Mees, A.,Klar, T. (deposition date: 2004-05-26, release date: 2004-12-14, Last modification date: 2024-07-03) |
Primary citation | Mees, A.,Klar, T.,Gnau, P.,Hennecke, U.,Eker, A.P.M.,Carell, T.,Essen, L.-O. Crystal structure of a photolyase bound to a CPD-like DNA lesion after in situ repair Science, 306:1789-1793, 2004 Cited by PubMed 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 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. PubMed: 15576622DOI: 10.1126/science.1101598 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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