8C6B

Light SFX structure of D.m(6-4)photolyase at 20ps time delay

8C6B の概要

• エントリーDOI: 10.2210/pdb8c6b/pdb
• 分子名称: Cryptochrome-1, FLAVIN-ADENINE DINUCLEOTIDE, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: photolyase, sfx, fad, flavoprotein
• 由来する生物種: Drosophila melanogaster (fruit fly)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 58957.45

構造登録者

Cellini, A.,Kumar, M.,Nimmrich, A.,Mutisya, J.,Furrer, A.,Beale, E.V.,Carrillo, M.,Malla, T.N.,Maj, P.,Dworkowskic, F.,Cirelli, C.,Ozerovi, D.,Bacellar, C.,Strandfuss, J.,Weinert, T.,Ihalainen, J.A.,Yuan Wahlgren, W.,Westenhoff, S. (登録日: 2023-01-11, 公開日: 2023-11-01, 最終更新日: 2024-05-15)

主引用文献

Cellini, A.,Shankar, M.K.,Nimmrich, A.,Hunt, L.A.,Monrroy, L.,Mutisya, J.,Furrer, A.,Beale, E.V.,Carrillo, M.,Malla, T.N.,Maj, P.,Vrhovac, L.,Dworkowski, F.,Cirelli, C.,Johnson, P.J.M.,Ozerov, D.,Stojkovic, E.A.,Hammarstrom, L.,Bacellar, C.,Standfuss, J.,Maj, M.,Schmidt, M.,Weinert, T.,Ihalainen, J.A.,Wahlgren, W.Y.,Westenhoff, S.
Directed ultrafast conformational changes accompany electron transfer in a photolyase as resolved by serial crystallography.
Nat.Chem., 16:624-632, 2024

PubMed Abstract: Charge-transfer reactions in proteins are important for life, such as in photolyases which repair DNA, but the role of structural dynamics remains unclear. Here, using femtosecond X-ray crystallography, we report the structural changes that take place while electrons transfer along a chain of four conserved tryptophans in the Drosophila melanogaster (6-4) photolyase. At femto- and picosecond delays, photoreduction of the flavin by the first tryptophan causes directed structural responses at a key asparagine, at a conserved salt bridge, and by rearrangements of nearby water molecules. We detect charge-induced structural changes close to the second tryptophan from 1 ps to 20 ps, identifying a nearby methionine as an active participant in the redox chain, and from 20 ps around the fourth tryptophan. The photolyase undergoes highly directed and carefully timed adaptations of its structure. This questions the validity of the linear solvent response approximation in Marcus theory and indicates that evolution has optimized fast protein fluctuations for optimal charge transfer.

PubMed: 38225270
DOI: 10.1038/s41557-023-01413-9

実験手法

X-RAY DIFFRACTION (1.9 Å)