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7YEC

TR-SFX MmCPDII-DNA complex: 6 ns snapshot. Includes 6 ns, dark, and extrapolated structure factors

7YEC の概要
エントリーDOI10.2210/pdb7yec/pdb
関連するPDBエントリー7YC7 7YCM 7YCP 7YCR 7YD6 7YD7 7YD8 7YDZ 7YE0 7YEB
分子名称Deoxyribodipyrimidine photolyase, CPD photolesion containing DNA, complementary oligonucleotide to the CPD containing DNA, ... (7 entities in total)
機能のキーワードflavoprotein, photolyase, light driven electron transfer, dna repair, time-resolved serial crystallography., dna binding protein
由来する生物種Methanosarcina mazei
詳細
タンパク質・核酸の鎖数6
化学式量合計129665.68
構造登録者
主引用文献Maestre-Reyna, M.,Wang, P.H.,Nango, E.,Hosokawa, Y.,Saft, M.,Furrer, A.,Yang, C.H.,Gusti Ngurah Putu, E.P.,Wu, W.J.,Emmerich, H.J.,Caramello, N.,Franz-Badur, S.,Yang, C.,Engilberge, S.,Wranik, M.,Glover, H.L.,Weinert, T.,Wu, H.Y.,Lee, C.C.,Huang, W.C.,Huang, K.F.,Chang, Y.K.,Liao, J.H.,Weng, J.H.,Gad, W.,Chang, C.W.,Pang, A.H.,Yang, K.C.,Lin, W.T.,Chang, Y.C.,Gashi, D.,Beale, E.,Ozerov, D.,Nass, K.,Knopp, G.,Johnson, P.J.M.,Cirelli, C.,Milne, C.,Bacellar, C.,Sugahara, M.,Owada, S.,Joti, Y.,Yamashita, A.,Tanaka, R.,Tanaka, T.,Luo, F.,Tono, K.,Zarzycka, W.,Muller, P.,Alahmad, M.A.,Bezold, F.,Fuchs, V.,Gnau, P.,Kiontke, S.,Korf, L.,Reithofer, V.,Rosner, C.J.,Seiler, E.M.,Watad, M.,Werel, L.,Spadaccini, R.,Yamamoto, J.,Iwata, S.,Zhong, D.,Standfuss, J.,Royant, A.,Bessho, Y.,Essen, L.O.,Tsai, M.D.
Visualizing the DNA repair process by a photolyase at atomic resolution.
Science, 382:eadd7795-eadd7795, 2023
Cited by
PubMed Abstract: Photolyases, a ubiquitous class of flavoproteins, use blue light to repair DNA photolesions. In this work, we determined the structural mechanism of the photolyase-catalyzed repair of a cyclobutane pyrimidine dimer (CPD) lesion using time-resolved serial femtosecond crystallography (TR-SFX). We obtained 18 snapshots that show time-dependent changes in four reaction loci. We used these results to create a movie that depicts the repair of CPD lesions in the picosecond-to-nanosecond range, followed by the recovery of the enzymatic moieties involved in catalysis, completing the formation of the fully reduced enzyme-product complex at 500 nanoseconds. Finally, back-flip intermediates of the thymine bases to reanneal the DNA were captured at 25 to 200 microseconds. Our data cover the complete molecular mechanism of a photolyase and, importantly, its chemistry and enzymatic catalysis at work across a wide timescale and at atomic resolution.
PubMed: 38033054
DOI: 10.1126/science.add7795
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.2 Å)
構造検証レポート
Validation report summary of 7yec
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-10-30に公開中

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