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Publication Abstract from PubMed

(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 A 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 A 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.

The three-dimensional structure of Drosophila melanogaster (6-4) photolyase at room temperature.,Cellini A, Yuan Wahlgren W, Henry L, Pandey S, Ghosh S, Castillon L, Claesson E, Takala H, Kubel J, Nimmrich A, Kuznetsova V, Nango E, Iwata S, Owada S, Stojkovic EA, Schmidt M, Ihalainen JA, Westenhoff S Acta Crystallogr D Struct Biol. 2021 Aug 1;77(Pt 8):1001-1009. doi:, 10.1107/S2059798321005830. Epub 2021 Jul 29. PMID:34342273^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.