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dc.contributor.authorBjörling, Alexander
dc.contributor.authorBerntsson, Oskar
dc.contributor.authorLehtivuori, Heli
dc.contributor.authorTakala, Heikki
dc.contributor.authorHughes, Ashley J.
dc.contributor.authorPanman, Matthijs
dc.contributor.authorHoernke, Maria
dc.contributor.authorNiebling, Stephan
dc.contributor.authorHenry, Léocadie
dc.contributor.authorHenning, Robert
dc.contributor.authorKosheleva, Irina
dc.contributor.authorChukharev, Vladimir
dc.contributor.authorTkachenko, Nikolai V.
dc.contributor.authorMenzel, Andreas
dc.contributor.authorNewby, Gemma
dc.contributor.authorKhakhulin, Dmitry
dc.contributor.authorWulff, Michael
dc.contributor.authorIhalainen, Janne
dc.contributor.authorWestenhoff, Sebastian
dc.date.accessioned2016-08-24T08:23:47Z
dc.date.available2016-08-24T08:23:47Z
dc.date.issued2016
dc.identifier.citationBjörling, A., Berntsson, O., Lehtivuori, H., Takala, H., Hughes, A. J., Panman, M., Hoernke, M., Niebling, S., Henry, L., Henning, R., Kosheleva, I., Chukharev, V., Tkachenko, N. V., Menzel, A., Newby, G., Khakhulin, D., Wulff, M., Ihalainen, J., & Westenhoff, S. (2016). Structural photoactivation of a full-length bacterial phytochrome. <i>Science Advances</i>, <i>2</i>(8), Article e1600920. <a href="https://doi.org/10.1126/sciadv.1600920" target="_blank">https://doi.org/10.1126/sciadv.1600920</a>
dc.identifier.otherCONVID_26179760
dc.identifier.otherTUTKAID_70992
dc.identifier.urihttps://jyx.jyu.fi/handle/123456789/51032
dc.description.abstractPhytochromes are light sensor proteins found in plants, bacteria, and fungi. They function by converting a photon absorption event into a conformational signal that propagates from the chromophore through the entire protein. However, the structure of the photoactivated state and the conformational changes that lead to it are not known. We report time-resolved x-ray scattering of the full-length phytochrome from Deinococcus radiodurans on micro- and millisecond time scales. We identify a twist of the histidine kinase output domains with respect to the chromophore-binding domains as the dominant change between the photoactivated and resting states. The time-resolved data further show that the structural changes up to the microsecond time scales are small and localized in the chromophore-binding domains. The global structural change occurs within a few milliseconds, coinciding with the formation of the spectroscopic meta-Rc state. Our findings establish key elements of the signaling mechanism of full-length bacterial phytochromes.
dc.language.isoeng
dc.publisherAmerican Association for the Advancement of Science
dc.relation.ispartofseriesScience Advances
dc.rightsCC BY 4.0
dc.subject.otherphytochromes
dc.subject.otherphotoactivation
dc.subject.otherDeinococcus radiodurans
dc.titleStructural photoactivation of a full-length bacterial phytochrome
dc.typearticle
dc.identifier.urnURN:NBN:fi:jyu-201608233853
dc.contributor.laitosBio- ja ympäristötieteiden laitosfi
dc.contributor.laitosFysiikan laitosfi
dc.contributor.laitosDepartment of Biological and Environmental Scienceen
dc.contributor.laitosDepartment of Physicsen
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.date.updated2016-08-23T12:15:06Z
dc.type.coarjournal article
dc.description.reviewstatuspeerReviewed
dc.relation.issn2375-2548
dc.relation.numberinseries8
dc.relation.volume2
dc.type.versionpublishedVersion
dc.rights.copyright© The Authors, 2016.
dc.rights.accesslevelopenAccessfi
dc.rights.urlhttps://creativecommons.org/licenses/by-nc/4.0/
dc.relation.doi10.1126/sciadv.1600920


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