8OYC

Time-resolved SFX structure of the class II photolyase complexed with a thymine dimer (100 microsecond timpeoint)

8OYC の概要

• エントリーDOI: 10.2210/pdb8oyc/pdb
• 分子名称: Deoxyribodipyrimidine photo-lyase, CPD-COMPRISING OLIGONUCLEOTIDE, COUNTERSTRAND-OLIGONUCLEOTIDE, ... (6 entities in total)
• 機能のキーワード: dna binding protein, dna repair enzyme, flavoprotein, photoenzyme, lyase
• 由来する生物種: Methanosarcina mazei Go1; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 132875.81

構造登録者

Lane, T.J.,Christou, N.-E.,Melo, D.V.M.,Apostolopoulou, V.,Pateras, A.,Mashhour, A.R.,Galchenkova, M.,Gunther, S.,Reinke, P.,Kremling, V.,Oberthuer, D.,Henkel, A.,Sprenger, J.,Scheer, T.E.S.,Lange, E.,Yefanov, O.N.,Middendorf, P.,Sellberg, J.A.,Schubert, R.,Fadini, A.,Cirelli, C.,Beale, E.V.,Johnson, P.,Dworkowski, F.,Ozerov, D.,Bertrand, Q.,Wranik, M.,Zitter, E.D.,Turk, D.,Bajt, S.,Chapman, H.,Bacellar, C. (登録日: 2023-05-03, 公開日: 2023-11-22, 最終更新日: 2023-12-13)

主引用文献

Christou, N.E.,Apostolopoulou, V.,Melo, D.V.M.,Ruppert, M.,Fadini, A.,Henkel, A.,Sprenger, J.,Oberthuer, D.,Gunther, S.,Pateras, A.,Rahmani Mashhour, A.,Yefanov, O.M.,Galchenkova, M.,Reinke, P.Y.A.,Kremling, V.,Scheer, T.E.S.,Lange, E.R.,Middendorf, P.,Schubert, R.,De Zitter, E.,Lumbao-Conradson, K.,Herrmann, J.,Rahighi, S.,Kunavar, A.,Beale, E.V.,Beale, J.H.,Cirelli, C.,Johnson, P.J.M.,Dworkowski, F.,Ozerov, D.,Bertrand, Q.,Wranik, M.,Bacellar, C.,Bajt, S.,Wakatsuki, S.,Sellberg, J.A.,Huse, N.,Turk, D.,Chapman, H.N.,Lane, T.J.
Time-resolved crystallography captures light-driven DNA repair.
Science, 382:1015-1020, 2023

PubMed Abstract: Photolyase is an enzyme that uses light to catalyze DNA repair. To capture the reaction intermediates involved in the enzyme's catalytic cycle, we conducted a time-resolved crystallography experiment. We found that photolyase traps the excited state of the active cofactor, flavin adenine dinucleotide (FAD), in a highly bent geometry. This excited state performs electron transfer to damaged DNA, inducing repair. We show that the repair reaction, which involves the lysis of two covalent bonds, occurs through a single-bond intermediate. The transformation of the substrate into product crowds the active site and disrupts hydrogen bonds with the enzyme, resulting in stepwise product release, with the 3' thymine ejected first, followed by the 5' base.

PubMed: 38033070
DOI: 10.1126/science.adj4270

実験手法

X-RAY DIFFRACTION (2.5 Å)