{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Jia H"],"funding":["National Natural Science Foundation of China","National Natural Science Foundation of China (National Science Foundation of China)"],"pagination":["51"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12098889"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["11(1)"],"pubmed_abstract":["The red/far-red light receptor phytochrome B (phyB) plays essential roles in regulating various plant development processes. PhyB exists in two distinct photoreversible forms: the inactive Pr form and the active Pfr form. phyB-Pfr binds phytochrome-interacting factors (PIFs) to transduce red light signals. Here, we determined the cryo-electron microscopy (cryo-EM) structures of the photoactivated phyB-Pfr‒PIF6 complex, the constitutively active mutant phyB<sup>Y276H</sup>‒PIF6 complex, and the truncated phyBN<sup>Y276H</sup>‒PIF6 complex. In these structures, two parallel phyB-Pfr molecules interact with one PIF6 molecule. Red light-triggered rotation of the PΦB D-ring leads to the conversion of hairpin loops into α helices and the \"head-to-head\" reassembly of phyB-Pfr N-terminal photosens"],"journal":["Cell discovery"],"pubmed_title":["Structural insight into PIF6-mediated red light signal transduction of plant phytochrome B."],"pmcid":["PMC12098889"],"funding_grant_id":["32400205","32071211"],"pubmed_authors":["Liu Z","Guan Z","Zhang D","Ma L","Zhu Y","Jia H","Yin P","Tian D","Wang X","Ding J"],"additional_accession":[]},"is_claimable":false,"name":"Structural insight into PIF6-mediated red light signal transduction of plant phytochrome B.","description":"The red/far-red light receptor phytochrome B (phyB) plays essential roles in regulating various plant development processes. PhyB exists in two distinct photoreversible forms: the inactive Pr form and the active Pfr form. phyB-Pfr binds phytochrome-interacting factors (PIFs) to transduce red light signals. Here, we determined the cryo-electron microscopy (cryo-EM) structures of the photoactivated phyB-Pfr‒PIF6 complex, the constitutively active mutant phyB<sup>Y276H</sup>‒PIF6 complex, and the truncated phyBN<sup>Y276H</sup>‒PIF6 complex. In these structures, two parallel phyB-Pfr molecules interact with one PIF6 molecule. Red light-triggered rotation of the PΦB D-ring leads to the conversion of hairpin loops into α helices and the \"head-to-head\" reassembly of phyB-Pfr N-terminal photosens","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 May","modification":"2026-06-02T20:46:27.171Z","creation":"2026-04-20T03:10:59.442Z"},"accession":"S-EPMC12098889","cross_references":{"pubmed":["40404641"],"doi":["10.1038/s41421-025-00802-3"]}}