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

dc.contributor.authorCellini, Andrea
dc.contributor.authorWahlgren, Weixiao Yuan
dc.contributor.authorHenry, Léocadie
dc.contributor.authorPandey, Suraj
dc.contributor.authorGhosh, Swagatha
dc.contributor.authorCastillon, Leticia
dc.contributor.authorClaesson, Elin
dc.contributor.authorTakala, Heikki
dc.contributor.authorKübel, Joachim
dc.contributor.authorNimmrich, Amke
dc.contributor.authorKuznetsova, Valentyna
dc.contributor.authorNango, Eriko
dc.contributor.authorIwata, So
dc.contributor.authorOwada, Shigeki
dc.contributor.authorStojković, Emina A.
dc.contributor.authorSchmidt, Marius
dc.contributor.authorIhalainen, Janne A.
dc.contributor.authorWestenhoff, Sebastian
dc.date.accessioned2021-08-04T12:18:30Z
dc.date.available2021-08-04T12:18:30Z
dc.date.issued2021
dc.identifier.citationCellini, 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. <i>Acta Crystallographica Section D : Structural Biology</i>, <i>77</i>(3), 1001-1009. <a href="https://doi.org/10.1107/s2059798321005830" target="_blank">https://doi.org/10.1107/s2059798321005830</a>
dc.identifier.otherCONVID_99149793
dc.identifier.urihttps://jyx.jyu.fi/handle/123456789/77286
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 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.en
dc.format.mimetypeapplication/pdf
dc.language.isoeng
dc.publisherWiley-Blackwell
dc.relation.ispartofseriesActa Crystallographica Section D : Structural Biology
dc.rightsCC BY 4.0
dc.subject.otherphotolyases
dc.subject.otherflavoproteins
dc.subject.otherFAD
dc.subject.otherserial crystallography
dc.subject.otherroom-temperature structure
dc.subject.otherDrosophila melanogaster
dc.subject.other(6–4) photolyase
dc.titleThe three-dimensional structure of Drosophila melanogaster (6–4) photolyase at room temperature
dc.typeresearch article
dc.identifier.urnURN:NBN:fi:jyu-202108044454
dc.contributor.laitosInformaatioteknologian tiedekuntafi
dc.contributor.laitosBio- ja ympäristötieteiden laitosfi
dc.contributor.laitosFaculty of Information Technologyen
dc.contributor.laitosDepartment of Biological and Environmental Scienceen
dc.contributor.oppiaineSolu- ja molekyylibiologiafi
dc.contributor.oppiaineNanoscience Centerfi
dc.contributor.oppiaineCell and Molecular Biologyen
dc.contributor.oppiaineNanoscience Centeren
dc.type.urihttp://purl.org/eprint/type/JournalArticle
dc.type.coarhttp://purl.org/coar/resource_type/c_2df8fbb1
dc.description.reviewstatuspeerReviewed
dc.format.pagerange1001-1009
dc.relation.issn2059-7983
dc.relation.numberinseries3
dc.relation.volume77
dc.type.versionpublishedVersion
dc.rights.copyright© 2021 the Authors
dc.rights.accesslevelopenAccessfi
dc.type.publicationarticle
dc.relation.grantnumber296135
dc.relation.grantnumber330678
dc.subject.ysokidetiede
dc.subject.ysoproteiinit
dc.subject.ysofotobiologia
dc.subject.ysoDNA
dc.subject.ysolämpötila
dc.subject.ysobanaanikärpänen
dc.format.contentfulltext
jyx.subject.urihttp://www.yso.fi/onto/yso/p643
jyx.subject.urihttp://www.yso.fi/onto/yso/p4332
jyx.subject.urihttp://www.yso.fi/onto/yso/p27666
jyx.subject.urihttp://www.yso.fi/onto/yso/p7690
jyx.subject.urihttp://www.yso.fi/onto/yso/p2100
jyx.subject.urihttp://www.yso.fi/onto/yso/p24873
dc.rights.urlhttps://creativecommons.org/licenses/by/4.0/
dc.relation.doi10.1107/s2059798321005830
dc.relation.funderResearch Council of Finlanden
dc.relation.funderResearch Council of Finlanden
dc.relation.funderSuomen Akatemiafi
dc.relation.funderSuomen Akatemiafi
jyx.fundingprogramAcademy Project, AoFen
jyx.fundingprogramAcademy Research Fellow, AoFen
jyx.fundingprogramAkatemiahanke, SAfi
jyx.fundingprogramAkatemiatutkija, SAfi
jyx.fundinginformationSW 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.
dc.type.okmA1


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