The three-dimensional structure of Drosophila melanogaster (6–4) photolyase at room temperature
Category
Published on
Type
journal-article
Author
Andrea Cellini and Weixiao Yuan Wahlgren and Léocadie Henry and Suraj Pandey and Swagatha Ghosh and Leticia Castillon and Elin Claesson and Heikki Takala and Joachim Kübel and Amke Nimmrich and Valentyna Kuznetsova and Eriko Nango and So Iwata and Shigeki Owada and Emina A. Stojković and Marius Schmidt and Janne A. Ihalainen and Sebastian Westenhoff
Citation
Cellini, A. et al., 2021. The three-dimensional structure of Drosophila melanogaster (6–4) photolyase at room temperature. Acta Crystallographica Section D Structural Biology, 77(8), pp.1001–1009. Available at: http://dx.doi.org/10.1107/s2059798321005830.
Abstract
(6–4) photolyases are flavoproteins that belong to the photolyase/cryptochrome family. Their function is to repair DNA lesions using visible light. Here, crystal structures of Drosophila melanogaster (6–4) photolyase [Dm(6–4)photolyase] at room and cryogenic temperatures are reported. The room-temperature structure was solved to 2.27 Å resolution and was obtained by serial femtosecond crystallography (SFX) using an X-ray free-electron laser. The crystallization and preparation conditions are also reported. The cryogenic structure was solved to 1.79 Å resolution using conventional X-ray crystallography. The structures agree with each other, indicating that the structural information obtained from crystallography at cryogenic temperature also applies at room temperature. Furthermore, UV–Vis absorption spectroscopy confirms that Dm(6–4)photolyase is photoactive in the crystals, giving a green light to time-resolved SFX studies on the protein, which can reveal the structural mechanism of the photoactivated protein in DNA repair.
DOI
Funding
NSF-STC Biology with X-ray Lasers (NSF-1231306)
