1TEZ

COMPLEX BETWEEN DNA AND THE DNA PHOTOLYASE FROM ANACYSTIS NIDULANS

1TEZ の概要

• エントリーDOI: 10.2210/pdb1tez/pdb
• 分子名称: 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)
• 機能のキーワード: photolyase; dna repair; light-driven electron transfer, lyase-dna complex, lyase/dna
• 由来する生物種: Synechococcus elongatus PCC 6301; 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 235903.52

構造登録者

Essen, L.-O.,Carell, T.,Mees, A.,Klar, T. (登録日: 2004-05-26, 公開日: 2004-12-14, 最終更新日: 2024-07-03)

主引用文献

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

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: 15576622
DOI: 10.1126/science.1101598

実験手法

X-RAY DIFFRACTION (1.8 Å)