0000000000298271

AUTHOR

Elin Claesson

showing 7 related works from this author

The primary structural photoresponse of phytochrome proteins captured by a femtosecond X-ray laser

2019

Phytochrome proteins control the growth, reproduction, and photosynthesis of plants, fungi, and bacteria. Light is detected by a bilin cofactor, but it remains elusive how this leads to activation of the protein through structural changes. We present serial femtosecond X-ray crystallographic data of the chromophore-binding domains of a bacterial phytochrome at delay times of 1 ps and 10 ps after photoexcitation. The data reveal a twist of the D-ring, which leads to partial detachment of the chromophore from the protein. Unexpectedly, the conserved so-called pyrrole water is photodissociated from the chromophore, concomitant with movement of the A-ring and a key signaling aspartate. The chan…

DYNAMICSQH301-705.5ScienceEXCITED-STATEDIFFRACTION010402 general chemistryPhotosynthesisphytochromes01 natural sciencesCofactor03 medical and health scienceschemistry.chemical_compoundDeinococcus radioduransPROTON-TRANSFERREVEALSSFXCRYSTAL-STRUCTUREBiology (General)Bilin030304 developmental biologyISOMERIZATION0303 health sciencesbiologyPhytochromeD-RINGChemistryCRYSTALLOGRAPHYinitial photoresponsQRChromophore0104 chemical sciencesPhotoexcitationFemtosecondbiology.proteinBiophysics1182 Biochemistry cell and molecular biologyMedicine3111 BiomedicinevalokemiaproteiinitSignal transductionröntgenkristallografia
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Author response: The primary structural photoresponse of phytochrome proteins captured by a femtosecond X-ray laser

2020

X-ray laserPrimary (chemistry)Materials sciencePhytochromebusiness.industryFemtosecondOptoelectronicsbusiness
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The three-dimensional structure of Drosophila melanogaster (6–4) photolyase at room temperature

2021

A crystal structure of a photolyase at room temperature confirms the structural information obtained from cryogenic crystallography and paves the way for time-resolved studies of the photolyase at an X-ray free-electron laser.

MECHANISMMaterials scienceAbsorption spectroscopyDNA repairfotobiologia02 engineering and technologyCrystal structureREPAIR ACTIVITY03 medical and health sciencesCOLI DNA PHOTOLYASEX-RAY-DIFFRACTIONCryptochromeStructural BiologyAnimalsserial crystallographyCRYSTAL-STRUCTURECRYPTOCHROMEPhotolyaseSERIAL FEMTOSECOND CRYSTALLOGRAPHY030304 developmental biology0303 health sciencesCrystallographyflavoproteinsFADResolution (electron density)TemperaturebanaanikärpänenDNAkidetiede(6-4) photolyase021001 nanoscience & nanotechnologyResearch PapersRADICAL TRANSFER(6–4) photolyaseroom-temperature structureCrystallographyphotolyasesDrosophila melanogasterRECONSTITUTIONX-ray crystallography1182 Biochemistry cell and molecular biologylämpötilaproteiinit0210 nano-technologyDeoxyribodipyrimidine Photo-LyasePHOTOACTIVATIONVisible spectrumActa Crystallographica Section D Structural Biology
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Structural mechanism of signal transduction in a phytochrome histidine kinase

2022

AbstractPhytochrome proteins detect red/far-red light to guide the growth, motion, development and reproduction in plants, fungi, and bacteria. Bacterial phytochromes commonly function as an entrance signal in two-component sensory systems. Despite the availability of three-dimensional structures of phytochromes and other two-component proteins, the conformational changes, which lead to activation of the protein, are not understood. We reveal cryo electron microscopy structures of the complete phytochrome from Deinoccocus radiodurans in its resting and photoactivated states at 3.6 Å and 3.5 Å resolution, respectively. Upon photoactivation, the photosensory core module hardly changes its ter…

Models MolecularkinaasitMultidisciplinaryphotochemistryHistidine KinaseLightBacteriaelectron microscopyBiochemistry and Molecular BiologyGeneral Physics and AstronomyelektronimikroskopiaGeneral ChemistryGeneral Biochemistry Genetics and Molecular BiologykinasesBacterial Proteinsplant signalling3111 BiomedicinePhytochromevalokemiaBiokemi och molekylärbiologiSignal Transduction
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Structural basis for light control of cell development revealed by crystal structures of a myxobacterial phytochrome

2018

Phytochromes are red-light photoreceptors that were first characterized in plants, with homologs in photosynthetic and non-photosynthetic bacteria known as bacteriophytochromes (BphPs). Upon absorption of light, BphPs interconvert between two states denoted Pr and Pfr with distinct absorption spectra in the red and far-red. They have recently been engineered as enzymatic photoswitches for fluorescent-marker applications in non-invasive tissue imaging of mammals. This article presents cryo- and room-temperature crystal structures of the unusual phytochrome from the non-photosynthetic myxobacterium Stigmatella aurantiaca (SaBphP1) and reveals its role in the fruiting-body formation of this ph…

MODULE0301 basic medicinePHOTOACTIVE YELLOW PROTEINSIGNALING MECHANISMabsorption spectraMutantfotobiologiaphytochromesBiochemistryyhteyttäminenbakteeritSTIGMATELLA-AURANTIACA03 medical and health sciencesFRUITING BODY FORMATIONGeneral Materials ScienceMolecular replacementStigmatella aurantiacalcsh:ScienceUNUSUAL BACTERIOPHYTOCHROMEPHOTOCONVERSIONHistidine030102 biochemistry & molecular biologybiologyPhytochromeChemistryCRYSTALLOGRAPHYta1182photosynthetic bacteriaphotoreceptorsGeneral ChemistryChromophoreCondensed Matter Physicsbiology.organism_classification030104 developmental biologyCHROMOPHORE-BINDING DOMAINBiophysicsmyxobacterialcsh:Q3111 BiomedicinePhotosynthetic bacteriaproteiinitMOLECULAR REPLACEMENTBinding domainIUCrJ
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Ultrafast structural changes within a photosynthetic reaction centre

2021

Nature <London> / Physical science 589, 310 - 314 (2021). doi:10.1038/s41586-020-3000-7

0301 basic medicinePhotosynthetic reaction centreChlorophyllModels MolecularklorofylliCytoplasmUbiquinonePhotosynthetic Reaction Center Complex ProteinsElectrons02 engineering and technologyPhotochemistrymedicine.disease_cause530yhteyttäminenbakteeritElectron Transport03 medical and health sciencesElectron transfermedicineMoleculeddc:530BacteriochlorophyllsbioenergetiikkaComputingMilieux_MISCELLANEOUSHyphomicrobiaceaeMultidisciplinaryBinding SitesCrystallography[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM]ChemistryBlastochloris viridisLaserskalvot (biologia)PheophytinsBiological membraneVitamin K 2021001 nanoscience & nanotechnologyAcceptor030104 developmental biologyPicosecondFemtosecondsense organsProtons0210 nano-technologyOxidation-Reductionröntgenkristallografia
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The primary structural photoresponse of phytochrome proteins captured by a femtosecond X-ray laser

2020

Please check the README file for more information about the dataset.

chromophore-binding domains of Bacterial phytochromeX-ray Free-electorn LasersXFELData_FILESBL3: EH2Serial Femtosecond CrystallographyGeneralLiterature_MISCELLANEOUSComputingMethodologies_COMPUTERGRAPHICSSACLA
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