Structural basis for the Pr-Pfr long-range signaling mechanism of a full-length bacterial phytochrome at the atomic level

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dc.contributor.authorOtero, Lisandro H.
dc.contributor.authorFoscaldi, Sabrina
dc.contributor.authorAntelo, Giuliano T.
dc.contributor.authorRosano, Germán L.
dc.contributor.authorSirigu, Serena
dc.contributor.authorKlinke, Sebastián
dc.contributor.authorDefelipe, Lucas A.
dc.contributor.authorSánchez-Lamas, Maximiliano
dc.contributor.authorBattocchio, Giovanni
dc.contributor.authorConforte, Valeria
dc.contributor.authorVojnov, Adrián A.
dc.contributor.authorChavas, Leonard M. G.
dc.contributor.authorGoldbaum, Fernando A.
dc.contributor.authorMroginski, Maria-Andrea
dc.contributor.authorRinaldi, Jimena
dc.contributor.authorBonomi, Hernán R.
dc.date.accessioned2022-02-07T14:50:02Z
dc.date.available2022-02-07T14:50:02Z
dc.date.issued2021-11-24
dc.description.abstractPhytochromes constitute a widespread photoreceptor family that typically interconverts between two photostates called Pr (red light–absorbing) and Pfr (far-red light–absorbing). The lack of full-length structures solved at the (near-)atomic level in both pure Pr and Pfr states leaves gaps in the structural mechanisms involved in the signal transmission pathways during the photoconversion. Here, we present the crystallographic structures of three versions from the plant pathogen Xanthomonas campestris virulence regulator XccBphP bacteriophytochrome, including two full-length proteins, in the Pr and Pfr states. The structures show a reorganization of the interaction networks within and around the chromophore-binding pocket, an α-helix/β-sheet tongue transition, and specific domain reorientations, along with interchanging kinks and breaks at the helical spine as a result of the photoswitching, which subsequently affect the quaternary assembly. These structural findings, combined with multidisciplinary studies, allow us to describe the signaling mechanism of a full-length bacterial phytochrome at the atomic level.en
dc.description.sponsorshipDFG, 221545957, SFB 1078: Proteinfunktion durch Protonierungsdynamiken
dc.description.sponsorshipEC/H2020/664726/EU/EMBL Interdisciplinary, International and Intersectorial Postdocs/EI3PODen
dc.identifier.eissn2375-2548
dc.identifier.urihttps://depositonce.tu-berlin.de/handle/11303/16303
dc.identifier.urihttp://dx.doi.org/10.14279/depositonce-15078
dc.language.isoenen
dc.rights.urihttps://creativecommons.org/licenses/by-nc/4.0/en
dc.subject.ddc540 Chemie und zugeordnete Wissenschaftende
dc.subject.otherPr-Pfr long-range signalingen
dc.subject.otherfull-length bacterial phytochromeen
dc.subject.otherphytochromesen
dc.subject.otherphotoreceptorsen
dc.subject.otheratomsen
dc.titleStructural basis for the Pr-Pfr long-range signaling mechanism of a full-length bacterial phytochrome at the atomic levelen
dc.typeArticleen
dc.type.versionpublishedVersionen
dcterms.bibliographicCitation.articlenumbereabh1097en
dcterms.bibliographicCitation.doi10.1126/sciadv.abh1097en
dcterms.bibliographicCitation.issue48en
dcterms.bibliographicCitation.journaltitleScience Advancesen
dcterms.bibliographicCitation.originalpublishernameAAASen
dcterms.bibliographicCitation.originalpublisherplaceWashington, DCen
dcterms.bibliographicCitation.volume7en
tub.accessrights.dnbfreeen
tub.affiliationFak. 2 Mathematik und Naturwissenschaften::Inst. Chemiede
tub.affiliation.facultyFak. 2 Mathematik und Naturwissenschaftende
tub.affiliation.instituteInst. Chemiede
tub.publisher.universityorinstitutionTechnische Universität Berlinen

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