7AYV
X-ray crystallographic structure of (6-4)photolyase from Drosophila melanogaster at cryogenic temperature
Summary for 7AYV
| Entry DOI | 10.2210/pdb7ayv/pdb |
| Descriptor | RE11660p, GLYCEROL, FLAVIN-ADENINE DINUCLEOTIDE, ... (5 entities in total) |
| Functional Keywords | flavoprotein, (6-4)photolyase, lyase |
| Biological source | Drosophila melanogaster (Fruit fly) |
| Total number of polymer chains | 1 |
| Total formula weight | 59671.00 |
| Authors | Cellini, A.,Wahlgren, W.Y.,Henry, L.,Westenhoff, S. (deposition date: 2020-11-13, release date: 2021-08-18, Last modification date: 2024-01-31) |
| Primary citation | 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, E.A.,Schmidt, M.,Ihalainen, J.A.,Westenhoff, S. The three-dimensional structure of Drosophila melanogaster (6-4) photolyase at room temperature. Acta Crystallogr D Struct Biol, 77:1001-1009, 2021 Cited by PubMed 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. PubMed: 34342273DOI: 10.1107/S2059798321005830 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.79 Å) |
Structure validation
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