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] atroom 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.
Highlights
Light plays an important role in plant and animal physiology
We solved the structure to 1.79 Aresolution by single-crystal crystallography at cryogenic temperature
We show that Dm(6–4)PL microcrystals suitable for SFX studies diffract to high resolution in order to observe conformational changes upon light activation
Summary
To name a few examples, light regulates development, deetiolation and flowering in plants (Liu et al, 2017; Putterill et al, 2004), and vision and vitamin D activation in animals (Holick, 2000; Lythgoe, 1984). To compensate for this, archaea, prokaryotes and eukaryotes have photolyase proteins, which repair damaged DNA using the energy of visible light (Sancar & Rupert, 1978; Sancar et al, 1987). Photolyases are members of the cryptochrome/photolyase photoreceptor family (Kavakli et al, 2017; Todo, 1999; Deisenhofer, 2000). While photolyases repair DNA, cryptochromes are circadian photoreceptors in plants that regulate growth and development
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