Publication Date:
2014-04-30
Description:
Sensory proteins must relay structural signals from the sensory site over large distances to regulatory output domains. Phytochromes are a major family of red-light-sensing kinases that control diverse cellular functions in plants, bacteria and fungi. Bacterial phytochromes consist of a photosensory core and a carboxy-terminal regulatory domain. Structures of photosensory cores are reported in the resting state and conformational responses to light activation have been proposed in the vicinity of the chromophore. However, the structure of the signalling state and the mechanism of downstream signal relay through the photosensory core remain elusive. Here we report crystal and solution structures of the resting and activated states of the photosensory core of the bacteriophytochrome from Deinococcus radiodurans. The structures show an open and closed form of the dimeric protein for the activated and resting states, respectively. This nanometre-scale rearrangement is controlled by refolding of an evolutionarily conserved 'tongue', which is in contact with the chromophore. The findings reveal an unusual mechanism in which atomic-scale conformational changes around the chromophore are first amplified into an angstrom-scale distance change in the tongue, and further grow into a nanometre-scale conformational signal. The structural mechanism is a blueprint for understanding how phytochromes connect to the cellular signalling network.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4015848/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉 〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4015848/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Takala, Heikki -- Bjorling, Alexander -- Berntsson, Oskar -- Lehtivuori, Heli -- Niebling, Stephan -- Hoernke, Maria -- Kosheleva, Irina -- Henning, Robert -- Menzel, Andreas -- Ihalainen, Janne A -- Westenhoff, Sebastian -- 1R24GM111072/GM/NIGMS NIH HHS/ -- 279944/European Research Council/International -- R24 GM111072/GM/NIGMS NIH HHS/ -- England -- Nature. 2014 May 8;509(7499):245-8. doi: 10.1038/nature13310. Epub 2014 Apr 30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉1] Nanoscience Center, Department of Biological and Environmental Science, University of Jyvaskyla, 40014 Jyvaskyla, Finland [2] Department of Chemistry and Molecular Biology, University of Gothenburg, 40530 Gothenburg, Sweden [3]. ; 1] Department of Chemistry and Molecular Biology, University of Gothenburg, 40530 Gothenburg, Sweden [2]. ; Department of Chemistry and Molecular Biology, University of Gothenburg, 40530 Gothenburg, Sweden. ; Nanoscience Center, Department of Biological and Environmental Science, University of Jyvaskyla, 40014 Jyvaskyla, Finland. ; Center for Advanced Radiation Sources, The University of Chicago, Illinois 60637, USA. ; Paul Scherrer Institut, 5232 Villigen PSI, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24776794" target="_blank"〉PubMed〈/a〉
Keywords:
Bacterial Proteins/*chemistry/*metabolism/radiation effects
;
Binding Sites
;
Crystallography, X-Ray
;
Deinococcus/*chemistry
;
*Light Signal Transduction/radiation effects
;
Models, Molecular
;
Phytochrome/chemistry/metabolism/radiation effects
;
Protein Conformation/radiation effects
Print ISSN:
0028-0836
Electronic ISSN:
1476-4687
Topics:
Biology
,
Chemistry and Pharmacology
,
Medicine
,
Natural Sciences in General
,
Physics
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