The three-dimensional structure of Drosophila melanogaster (6–4) photolyase at room temperature
Cellini, A., Wahlgren, W. Y., Henry, L., Pandey, S., Ghosh, S., Castillon, L., Claesson, E., Takala, H., Kübel, J., Nimmrich, A., Kuznetsova, V., Nango, E., Iwata, S., Owada, S., Stojković, E. A., Schmidt, M., Ihalainen, J. A., & Westenhoff, S. (2021). The three-dimensional structure of Drosophila melanogaster (6–4) photolyase at room temperature. Acta Crystallographica Section D : Structural Biology, 77(3), 1001-1009. https://doi.org/10.1107/s2059798321005830
© 2021 the Authors
(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. ...
ISSN Search the Publication Forum2059-7983
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Related funder(s)Academy of Finland
Funding program(s)Academy Project, AoF; Academy Research Fellow, AoF
Additional information about fundingSW acknowledges the European Research Council for support (Grant No. 279944). This work was supported by Academy of Finland grants 285461, 330678 (both to HT) and 296135 (to JAI) and the Jane and Aatos Erkko Foundation (JAI). This research was partially supported by the Platform Project for Supporting Drug Discovery and Life Science Research [Basis for Supporting Innovative Drug Discovery and Life Science Research (BINDS)] from the Japan Agency for Medical Research and Development (AMED; Grant No. JP20am0101070). This work was supported by National Science Foundation (NSF) Science and Technology Centers grant NSF-1231306 (‘Biology with X-ray Lasers’; MS) and research grants NSF-MCB-RUI 1413360 and NSF-MCBEAGER 1839513 to EAS. ...
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