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dc.contributor.authorBerntsson, Oskar
dc.contributor.authorDiensthuber, Ralph P.
dc.contributor.authorPanman, Matthijs R.
dc.contributor.authorBjörling, Alexander
dc.contributor.authorGustavsson, Emil
dc.contributor.authorHoernke, Maria
dc.contributor.authorHughes, Ashley J.
dc.contributor.authorHenry, Léocadie
dc.contributor.authorNiebling, Stephan
dc.contributor.authorTakala, Heikki
dc.contributor.authorIhalainen, Janne
dc.contributor.authorNewby, Gemma
dc.contributor.authorKerruth, Silke
dc.contributor.authorHeberle, Joachim
dc.contributor.authorLiebi, Marianne
dc.contributor.authorMenzel, Andreas
dc.contributor.authorHenning, Robert
dc.contributor.authorKosheleva, Irina
dc.contributor.authorMöglich, Andreas
dc.contributor.authorWestenhoff, Sebastian
dc.date.accessioned2017-09-01T11:26:40Z
dc.date.available2017-09-01T11:26:40Z
dc.date.issued2017
dc.identifier.citationBerntsson, O., Diensthuber, R. P., Panman, M. R., Björling, A., Gustavsson, E., Hoernke, M., . . . Westenhoff, S. (2017). Sequential conformational transitions and α-helical supercoiling regulate a sensor histidine kinase. <em>Nature Communications</em>, 8, 284. <a href="https://doi.org/10.1038/s41467-017-00300-5">doi:10.1038/s41467-017-00300-5</a>
dc.identifier.otherTUTKAID_74761
dc.identifier.urihttps://jyx.jyu.fi/handle/123456789/55249
dc.description.abstractSensor histidine kinases are central to sensing in bacteria and in plants. They usually contain sensor, linker, and kinase modules and the structure of many of these components is known. However, it is unclear how the kinase module is structurally regulated. Here, we use nano- to millisecond time-resolved X-ray scattering to visualize the solution structural changes that occur when the light-sensitive model histidine kinase YF1 is activated by blue light. We find that the coiled coil linker and the attached histidine kinase domains undergo a left handed rotation within microseconds. In a much slower second step, the kinase domains rearrange internally. This structural mechanism presents a template for signal transduction in sensor histidine kinases.
dc.language.isoeng
dc.publisherNature Publishing Group
dc.relation.ispartofseriesNature Communications
dc.subject.otherentsyymit
dc.subject.otherkinaasit
dc.subject.otheraktivointi
dc.subject.otherkinases
dc.subject.othersensor histidine kinases
dc.subject.otherphotoactivation
dc.titleSequential conformational transitions and α-helical supercoiling regulate a sensor histidine kinase
dc.typearticle
dc.identifier.urnURN:NBN:fi:jyu-201708243558
dc.contributor.laitosBio- ja ympäristötieteiden laitosfi
dc.contributor.laitosThe Department of Biological and Environmental Scienceen
dc.contributor.oppiaineSolu- ja molekyylibiologia
dc.type.urihttp://purl.org/eprint/type/JournalArticle
dc.date.updated2017-08-24T12:15:04Z
dc.type.coarjournal article
dc.description.reviewstatuspeerReviewed
dc.relation.issn2041-1723
dc.relation.volume8
dc.type.versionpublishedVersion
dc.rights.copyright© the Authors, 2017. This article is licensed under a Creative Commons Attribution 4.0 International License.
dc.rights.accesslevelopenAccessfi
dc.rights.urlhttps://creativecommons.org/licenses/by/4.0/
dc.relation.doi10.1038/s41467-017-00300-5


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© the Authors, 2017. This article is licensed under a Creative Commons Attribution 4.0 International License.
Except where otherwise noted, this item's license is described as © the Authors, 2017. This article is licensed under a Creative Commons Attribution 4.0 International License.