The three-dimensional structure of Drosophila melanogaster (6-4) photolyase at room temperature

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http://hdl.handle.net/10138/334682

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Cellini , A , Wahlgren , W Y , 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 2021 , ' The three-dimensional structure of Drosophila melanogaster (6-4) photolyase at room temperature ' , Acta crystallographica. Section D, Structural biology , vol. 77 , pp. 1001-1009 . https://doi.org/10.1107/S2059798321005830

Julkaisun nimi: The three-dimensional structure of Drosophila melanogaster (6-4) photolyase at room temperature
Tekijä: Cellini, Andrea; Wahlgren, Weixiao Yuan; Henry, Leocadie; Pandey, Suraj; Ghosh, Swagatha; Castillon, Leticia; Claesson, Elin; Takala, Heikki; Kubel, Joachim; Nimmrich, Amke; Kuznetsova, Valentyna; Nango, Eriko; Iwata, So; Owada, Shigeki; Stojkovic, Emina A.; Schmidt, Marius; Ihalainen, Janne A.; Westenhoff, Sebastian
Tekijän organisaatio: Medicum
Department of Anatomy
Päiväys: 2021-08-01
Kieli: eng
Sivumäärä: 9
Kuuluu julkaisusarjaan: Acta crystallographica. Section D, Structural biology
ISSN: 2059-7983
DOI-tunniste: https://doi.org/10.1107/S2059798321005830
URI: http://hdl.handle.net/10138/334682
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 angstrom 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 angstrom 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.
Avainsanat: photolyases
flavoproteins
FAD
serial crystallography
room-temperature structure
Drosophila melanogaster
(6-4) photolyase
SERIAL FEMTOSECOND CRYSTALLOGRAPHY
COLI DNA PHOTOLYASE
X-RAY-DIFFRACTION
CRYSTAL-STRUCTURE
RADICAL TRANSFER
REPAIR ACTIVITY
MECHANISM
CRYPTOCHROME
PHOTOACTIVATION
RECONSTITUTION
1182 Biochemistry, cell and molecular biology
Vertaisarvioitu: Kyllä
Pääsyrajoitteet: openAccess
Rinnakkaistallennettu versio: publishedVersion


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