9HNN

Structure of the (6-4) photolyase of Caulobacter crescentus in its fully reduced state determined by serial femtosecond crystallography

9HNN の概要

• エントリーDOI: 10.2210/pdb9hnn/pdb
• 分子名称: Cryptochrome/photolyase family protein, FLAVIN-ADENINE DINUCLEOTIDE, 1-deoxy-1-(6,7-dimethyl-2,4-dioxo-3,4-dihydropteridin-8(2H)-yl)-D-ribitol, ... (5 entities in total)
• 機能のキーワード: dna repair, photolyase, electron transfer, iron-sulfur cluster, flavoprotein
• 由来する生物種: Caulobacter vibrioides
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 59584.78

構造登録者

Po Hsun, W.,Maestre-Reyna, M.,Essen, L.-O. (登録日: 2024-12-11, 公開日: 2025-05-07, 最終更新日: 2025-05-21)

主引用文献

Wang, P.H.,Hosokawa, Y.,C Soares, J.,Emmerich, H.J.,Fuchs, V.,Caramello, N.,Engilberge, S.,Bologna, A.,Rosner, C.J.,Nakamura, M.,Watad, M.,Luo, F.,Owada, S.,Tosha, T.,Kang, J.,Tono, K.,Bessho, Y.,Nango, E.,Pierik, A.J.,Royant, A.,Tsai, M.D.,Yamamoto, J.,Maestre-Reyna, M.,Essen, L.O.
Redox-State-Dependent Structural Changes within a Prokaryotic 6-4 Photolyase.
J.Am.Chem.Soc., 147:16084-16098, 2025

PubMed Abstract: Photolyases repair UV damage to DNA by using absorbed blue light. Within the photolyase/cryptochrome superfamily (PCSf), a major subgroup consists of prokaryotic (6-4) photolyases. These enzymes rely on flavin adenine dinucleotide (FAD) as a catalytic cofactor, besides an ancillary antenna chromophore, and a [4Fe-4S] cluster with yet unknown function. For the prokaryotic 6-4 photolyase of , we investigated structural changes associated with its different redox states by damage-free crystallography using X-ray free-electron lasers. EPR and optical spectroscopy confirmed redox-dependent structural transitions, including the formation of an oxidized [4Fe-4S] cluster with the dynamic cleavage of a single iron-sulfur bond. Photoreduction to the catalytic FADH state alters the flavin binding site at the proximal aromatic pair Y390/F394 that is part of the electron transport pathway. Upon oxidation, the observable structural transitions of the protein matrix around the [4Fe-4S] cluster may affect DNA binding and are consistent with the much-debated role of the iron-sulfur cluster in DNA-binding proteins for quenching electron holes.

PubMed: 40298610
DOI: 10.1021/jacs.4c18116

実験手法

X-RAY DIFFRACTION (1.78 Å)