1tez
From Proteopedia
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[[Category: photolyase; dna repair; light-driven electron transfer]] | [[Category: photolyase; dna repair; light-driven electron transfer]] | ||
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Revision as of 15:00, 5 November 2007
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COMPLEX BETWEEN DNA AND THE DNA PHOTOLYASE FROM ANACYSTIS NIDULANS
Overview
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.
About this Structure
1TEZ is a Single protein structure of sequence from Synechococcus sp. with MG, FAD and HDF as ligands. Active as Deoxyribodipyrimidine photo-lyase, with EC number 4.1.99.3 Structure known Active Site: ACT. Full crystallographic information is available from OCA.
Reference
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
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