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dc.contributor.authorWoitowich, Nicole C.
dc.contributor.authorHalavaty, Andrei S.
dc.contributor.authorWaltz, Patricia
dc.contributor.authorKupitz, Christopher
dc.contributor.authorValera, Joseph
dc.contributor.authorTracy, Gregory
dc.contributor.authorGallagher, Kevin D.
dc.contributor.authorClaesson, Elin
dc.contributor.authorNakane, Takanori
dc.contributor.authorPandey, Suraj
dc.contributor.authorNelson, Garrett
dc.contributor.authorTanaka, Rie
dc.contributor.authorNango, Eriko
dc.contributor.authorMizohata, Eiichi
dc.contributor.authorOwada, Shigeki
dc.contributor.authorTono, Kensure
dc.contributor.authorJoti, Yasumasa
dc.contributor.authorNugent, Angela C.
dc.contributor.authorPatel, Hardik
dc.contributor.authorMapara, Ayesha
dc.contributor.authorHopkins, James
dc.contributor.authorDuong, Phu
dc.contributor.authorBizhga, Dorina
dc.contributor.authorKovaleva, Svetlana E.
dc.contributor.authorPeter, Rachael St.
dc.contributor.authorHernandez, Cynthia N.
dc.contributor.authorOzarowski, Wesley B.
dc.contributor.authorRoy-Chowdhuri, Shatabdi
dc.contributor.authorYang, Jay-How
dc.contributor.authorEdlund, Petra
dc.contributor.authorTakala, Heikki
dc.contributor.authorIhalainen, Janne
dc.contributor.authorBrayshaw, Jennifer
dc.contributor.authorNorwood, Tyler
dc.contributor.authorPoudyal, Ishwor
dc.contributor.authorFromme, Petra
dc.contributor.authorSpence, John C. H.
dc.contributor.authorMoffat, Keith
dc.contributor.authorWestenhoff, Sebastian
dc.contributor.authorSchmidt, Marius
dc.contributor.authorStojković, Emina A.
dc.date.accessioned2018-09-26T07:22:16Z
dc.date.available2018-09-26T07:22:16Z
dc.date.issued2018
dc.identifier.citationWoitowich, N. C., Halavaty, A. S., Waltz, P., Kupitz, C., Valera, J., Tracy, G., Gallagher, K. D., Claesson, E., Nakane, T., Pandey, S., Nelson, G., Tanaka, R., Nango, E., Mizohata, E., Owada, S., Tono, K., Joti, Y., Nugent, A. C., Patel, H., . . . Stojković, E. A. (2018). Structural basis for light control of cell development revealed by crystal structures of a myxobacterial phytochrome. <i>IUCrJ</i>, <i>5</i>(5), 619-634. <a href="https://doi.org/10.1107/S2052252518010631" target="_blank">https://doi.org/10.1107/S2052252518010631</a>
dc.identifier.otherCONVID_28281809
dc.identifier.otherTUTKAID_78946
dc.identifier.urihttps://jyx.jyu.fi/handle/123456789/59673
dc.description.abstractPhytochromes 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 photomorphogenic bacterium. SaBphP1 lacks a conserved histidine (His) in the chromophore-binding domain that stabilizes the Pr state in the classical BphPs. Instead it contains a threonine (Thr), a feature that is restricted to several myxobacterial phytochromes and is not evolutionarily understood. SaBphP1 structures of the chromophore binding domain (CBD) and the complete photosensory core module (PCM) in wild-type and Thr-to-His mutant forms reveal details of the molecular mechanism of the Pr/Pfr transition associated with the physiological response of this myxobacterium to red light. Specifically, key structural differences in the CBD and PCM between the wild-type and the Thr-to-His mutant involve essential chromophore contacts with proximal amino acids, and point to how the photosignal is transduced through the rest of the protein, impacting the essential enzymatic activity in the photomorphogenic response of this myxobacterium.en
dc.format.mimetypeapplication/pdf
dc.language.isoeng
dc.publisherInternational Union of Crystallography
dc.relation.ispartofseriesIUCrJ
dc.rightsCC BY 2.0
dc.subject.otherphytochromes
dc.subject.otherphotoreceptors
dc.subject.otherphotosynthetic bacteria
dc.subject.othermyxobacteria
dc.subject.otherabsorption spectra
dc.titleStructural basis for light control of cell development revealed by crystal structures of a myxobacterial phytochrome
dc.typearticle
dc.identifier.urnURN:NBN:fi:jyu-201809254233
dc.contributor.laitosBio- ja ympäristötieteiden laitosfi
dc.contributor.laitosDepartment of Biological and Environmental Scienceen
dc.contributor.oppiaineSolu- ja molekyylibiologiafi
dc.contributor.oppiaineNanoscience Centerfi
dc.contributor.oppiaineCell and Molecular Biologyen
dc.contributor.oppiaineNanoscience Centeren
dc.type.urihttp://purl.org/eprint/type/JournalArticle
dc.date.updated2018-09-25T09:15:09Z
dc.description.reviewstatuspeerReviewed
dc.format.pagerange619-634
dc.relation.issn2052-2525
dc.relation.numberinseries5
dc.relation.volume5
dc.type.versionpublishedVersion
dc.rights.copyright© 2018 the Authors
dc.rights.accesslevelopenAccessfi
dc.relation.grantnumber296135
dc.subject.ysoproteiinit
dc.subject.ysoyhteyttäminen
dc.subject.ysofotobiologia
dc.subject.ysobakteerit
dc.format.contentfulltext
jyx.subject.urihttp://www.yso.fi/onto/yso/p4332
jyx.subject.urihttp://www.yso.fi/onto/yso/p3008
jyx.subject.urihttp://www.yso.fi/onto/yso/p27666
jyx.subject.urihttp://www.yso.fi/onto/yso/p1749
dc.rights.urlhttps://creativecommons.org/licenses/by/2.0/uk/legalcode
dc.relation.doi10.1107/S2052252518010631
dc.relation.funderSuomen Akatemiafi
dc.relation.funderAcademy of Finlanden
jyx.fundingprogramAkatemiahanke, SAfi
jyx.fundingprogramAcademy Project, AoFen
jyx.fundinginformationThis work was supported by NSF-STC `BioXFEL' (STC-1231306). E. A. Stojkovic was supported by NSF RUI grant BIO-MCB 1413360 and NIH grant T34 GM105549-01 NU-STARS. K. Moffat was supported by NIH grant EY024363. S. Westenhoff acknowledges support by the European Research Council, contract number 279944. The Academy of Finland is acknowledged for grants 296135 (J. Ihalainen) and 285461 (H. Takala). P. Fromme and S. Roy-Chowdhuri also acknowledge support from the NIH Femtosecond Nano-crystallography of Membrane Proteins (No. R01GM095583). J. Ihalainen and S. Westenhoff acknowledge support by the Swedish Foundation for International Cooperation in Research and Higher Education.


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