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

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dc.contributor.author Cellini, Andrea
dc.contributor.author Wahlgren, Weixiao Yuan
dc.contributor.author Henry, Leocadie
dc.contributor.author Pandey, Suraj
dc.contributor.author Ghosh, Swagatha
dc.contributor.author Castillon, Leticia
dc.contributor.author Claesson, Elin
dc.contributor.author Takala, Heikki
dc.contributor.author Kubel, Joachim
dc.contributor.author Nimmrich, Amke
dc.contributor.author Kuznetsova, Valentyna
dc.contributor.author Nango, Eriko
dc.contributor.author Iwata, So
dc.contributor.author Owada, Shigeki
dc.contributor.author Stojkovic, Emina A.
dc.contributor.author Schmidt, Marius
dc.contributor.author Ihalainen, Janne A.
dc.contributor.author Westenhoff, Sebastian
dc.date.accessioned 2021-09-28T22:45:54Z
dc.date.available 2021-09-28T22:45:54Z
dc.date.issued 2021-08-01
dc.identifier.citation 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
dc.identifier.other PURE: 168813127
dc.identifier.other PURE UUID: e11388c0-ce02-463f-a01d-9a3b5990e9e5
dc.identifier.other WOS: 000681698200003
dc.identifier.other ORCID: /0000-0003-2518-8583/work/100697182
dc.identifier.uri http://hdl.handle.net/10138/334682
dc.description.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 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. en
dc.format.extent 9
dc.language.iso eng
dc.relation.ispartof Acta crystallographica. Section D, Structural biology
dc.rights.uri info:eu-repo/semantics/openAccess
dc.subject photolyases
dc.subject flavoproteins
dc.subject FAD
dc.subject serial crystallography
dc.subject room-temperature structure
dc.subject Drosophila melanogaster
dc.subject (6-4) photolyase
dc.subject SERIAL FEMTOSECOND CRYSTALLOGRAPHY
dc.subject COLI DNA PHOTOLYASE
dc.subject X-RAY-DIFFRACTION
dc.subject CRYSTAL-STRUCTURE
dc.subject RADICAL TRANSFER
dc.subject REPAIR ACTIVITY
dc.subject MECHANISM
dc.subject CRYPTOCHROME
dc.subject PHOTOACTIVATION
dc.subject RECONSTITUTION
dc.subject 1182 Biochemistry, cell and molecular biology
dc.title The three-dimensional structure of Drosophila melanogaster (6-4) photolyase at room temperature en
dc.type Article
dc.contributor.organization Medicum
dc.contributor.organization Department of Anatomy
dc.description.reviewstatus Peer reviewed
dc.relation.doi https://doi.org/10.1107/S2059798321005830
dc.relation.issn 2059-7983
dc.rights.accesslevel openAccess
dc.type.version publishedVersion

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