Näytä suppeat kuvailutiedot

dc.contributor.authorTakala, Heikki
dc.contributor.authorNiebling, Stephan
dc.contributor.authorBerntsson, Oskar
dc.contributor.authorBjörling, Alexander
dc.contributor.authorLehtivuori, Heli
dc.contributor.authorHäkkänen, Heikki
dc.contributor.authorPanman, Matthijs
dc.contributor.authorGustavsson, Emil
dc.contributor.authorHoernke, Maria
dc.contributor.authorNewby, Gemma
dc.contributor.authorZontone, Federico
dc.contributor.authorWulff, Michael
dc.contributor.authorMenzel, Andreas
dc.contributor.authorIhalainen, Janne
dc.contributor.authorWestenhoff, Sebastian
dc.date.accessioned2016-10-04T11:08:14Z
dc.date.available2016-10-04T11:08:14Z
dc.date.issued2016
dc.identifier.citationTakala, H., Niebling, S., Berntsson, O., Björling, A., Lehtivuori, H., Häkkänen, H., Panman, M., Gustavsson, E., Hoernke, M., Newby, G., Zontone, F., Wulff, M., Menzel, A., Ihalainen, J., & Westenhoff, S. (2016). Light-induced structural changes in a monomeric bacteriophytochrome. <i>Structural Dynamics</i>, <i>3</i>(5), Article 054701. <a href="https://doi.org/10.1063/1.4961911" target="_blank">https://doi.org/10.1063/1.4961911</a>
dc.identifier.otherCONVID_26243058
dc.identifier.otherTUTKAID_71328
dc.identifier.urihttps://jyx.jyu.fi/handle/123456789/51531
dc.description.abstractPhytochromes sense red light in plants and various microorganism. Light absorption causes structural changes within the protein, which alter its biochemical activity. Bacterial phytochromes are dimeric proteins, but the functional relevance of this arrangement remains unclear. Here, we use time-resolved X-ray scattering to reveal the solution structural change of a monomeric variant of the photosensory core module of the phytochrome from Deinococcus radiodurans. The data reveal two motions, a bend and a twist of the PHY domain with respect to the chromophore-binding domains. Infrared spectroscopy shows the refolding of the PHY tongue. We conclude that a monomer of the phytochrome photosensory core is sufficient to perform the light-induced structural changes. This implies that allosteric cooperation with the other monomer is not needed for structural activation. The dimeric arrangement may instead be intrinsic to the biochemical output domains of bacterial phytochromes.
dc.language.isoeng
dc.publisherAmerican Crystallographic Association; AIP Publishing
dc.relation.ispartofseriesStructural Dynamics
dc.subject.otherbacterial phytochromes
dc.titleLight-induced structural changes in a monomeric bacteriophytochrome
dc.typearticle
dc.identifier.urnURN:NBN:fi:jyu-201610034249
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.oppiaineFysiikkafi
dc.contributor.oppiaineNanoscience Centerfi
dc.contributor.oppiaineCell and Molecular Biologyen
dc.contributor.oppiainePhysicsen
dc.contributor.oppiaineNanoscience Centeren
dc.type.urihttp://purl.org/eprint/type/JournalArticle
dc.date.updated2016-10-03T09:15:04Z
dc.type.coarhttp://purl.org/coar/resource_type/c_2df8fbb1
dc.description.reviewstatuspeerReviewed
dc.relation.issn2329-7778
dc.relation.numberinseries5
dc.relation.volume3
dc.type.versionpublishedVersion
dc.rights.copyright© Author(s) 2016. This is an open access article distributed under the terms of a Creative Commons License.
dc.rights.accesslevelopenAccessfi
dc.rights.urlhttps://creativecommons.org/licenses/by/4.0/
dc.relation.doi10.1063/1.4961911
dc.type.okmA1


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Näytä suppeat kuvailutiedot

© Author(s) 2016. This is an open access article distributed under the terms of a Creative Commons License.
Ellei muuten mainita, aineiston lisenssi on © Author(s) 2016. This is an open access article distributed under the terms of a Creative Commons License.