Structural photoactivation of a full-length bacterial phytochrome
| العنوان: | Structural photoactivation of a full-length bacterial phytochrome |
|---|---|
| المؤلفون: | Matthijs R. Panman, Maria Hoernke, Vladimir Chukharev, Irina Kosheleva, Oskar Berntsson, Alexander Björling, Dmitry Khakhulin, Heikki Takala, Janne A. Ihalainen, Léocadie Henry, Gemma Newby, Andreas Menzel, Stephan Niebling, Michael Wulff, Sebastian Westenhoff, Heli Lehtivuori, Nikolai V. Tkachenko, Ashley J. Hughes, Robert Henning |
| المساهمون: | Tampere University, Department of Chemistry and Bioengineering, Research group: Supramolecular photochemistry, Biophysics Photosynthesis/Energy |
| المصدر: | Bjorling, 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 A & Westenhoff, S 2016, ' Structural photoactivation of a full-length bacterial phytochrome ', Science advances, vol. 2, no. 8 . https://doi.org/10.1126/sciadv.1600920 'Science Advances ', vol: 2, pages: e1600920-1-e1600920-10 (2016) Science Advances Science advances, 2(8). American Association for the Advancement of Science |
| بيانات النشر: | American Association for the Advancement of Science, 2016. |
| سنة النشر: | 2016 |
| مصطلحات موضوعية: | Models, Molecular, 0301 basic medicine, Protein Conformation, Astrophysics::High Energy Astrophysical Phenomena, 116 Chemical sciences, Photoreceptors, Microbial, phytochromes, Quantitative Biology::Cell Behavior, Structure-Activity Relationship, 03 medical and health sciences, Protein structure, Bacterial Proteins, Structural Biology, Deinococcus radiodurans, Botany, Research Articles, 219 Environmental biotechnology, Multidisciplinary, biology, Phytochrome, Histidine kinase, ta1182, SciAdv r-articles, Chromophore, biology.organism_classification, Kinetics, Microsecond, 030104 developmental biology, Structural change, photoactivation, Biophysics, Function (biology), Research Article |
| الوصف: | Time-resolved x-ray solution scattering reveals the conformational signaling mechanism of a bacterial phytochrome. Phytochromes 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. |
| وصف الملف: | application/pdf; fulltext |
| اللغة: | English |
| تدمد: | 2375-2548 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bd2c9b9da653ab9d91c005cad615e70a http://urn.fi/URN:NBN:fi:jyu-201608233853 |
| حقوق: | OPEN |
| رقم الأكسشن: | edsair.doi.dedup.....bd2c9b9da653ab9d91c005cad615e70a |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 23752548 |
|---|