A1 Alkuperäisartikkeli tieteellisessä aikakauslehdessä
The three-dimensional structure of Drosophila melanogaster (6–4) photolyase at room temperature (2021)


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


JYU-tekijät tai -toimittajat


Julkaisun tiedot

Julkaisun kaikki tekijät tai toimittajat: Cellini, Andrea; Wahlgren, Weixiao Yuan; Henry, Léocadie; Pandey, Suraj; Ghosh, Swagatha; Castillon, Leticia; Claesson, Elin; Takala, Heikki; Kübel, Joachim; Nimmrich, Amke; et al.

Lehti tai sarja: Acta Crystallographica Section D : Structural Biology

eISSN: 2059-7983

Julkaisuvuosi: 2021

Ilmestymispäivä: 29.07.2021

Volyymi: 77

Lehden numero: 3

Artikkelin sivunumerot: 1001-1009

Kustantaja: Wiley-Blackwell

Julkaisumaa: Yhdysvallat (USA)

Julkaisun kieli: englanti

DOI: https://doi.org/10.1107/s2059798321005830

Julkaisun avoin saatavuus: Avoimesti saatavilla

Julkaisukanavan avoin saatavuus: Osittain avoin julkaisukanava

Julkaisu on rinnakkaistallennettu (JYX): https://jyx.jyu.fi/handle/123456789/77286


Tiivistelmä

(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.


YSO-asiasanat: kidetiede; proteiinit; DNA; lämpötila; banaanikärpänen; fotobiologia

Vapaat asiasanat: photolyases; flavoproteins; FAD; serial crystallography; room-temperature structure; Drosophila melanogaster; (6–4) photolyase


Liittyvät organisaatiot


Hankkeet, joissa julkaisu on tehty


OKM-raportointi: Kyllä

Raportointivuosi: 2021

JUFO-taso: 1


Viimeisin päivitys 2024-03-04 klo 19:55