<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Jia H</submitter><funding>National Natural Science Foundation of China</funding><funding>National Natural Science Foundation of China (National Science Foundation of China)</funding><pagination>51</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC12098889</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>11(1)</volume><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&lt;sup>Y276H&lt;/sup>‒PIF6 complex, and the truncated phyBN&lt;sup>Y276H&lt;/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</pubmed_abstract><journal>Cell discovery</journal><pubmed_title>Structural insight into PIF6-mediated red light signal transduction of plant phytochrome B.</pubmed_title><pmcid>PMC12098889</pmcid><funding_grant_id>32400205</funding_grant_id><funding_grant_id>32071211</funding_grant_id><pubmed_authors>Liu Z</pubmed_authors><pubmed_authors>Guan Z</pubmed_authors><pubmed_authors>Zhang D</pubmed_authors><pubmed_authors>Ma L</pubmed_authors><pubmed_authors>Zhu Y</pubmed_authors><pubmed_authors>Jia H</pubmed_authors><pubmed_authors>Yin P</pubmed_authors><pubmed_authors>Tian D</pubmed_authors><pubmed_authors>Wang X</pubmed_authors><pubmed_authors>Ding J</pubmed_authors></additional><is_claimable>false</is_claimable><name>Structural insight into PIF6-mediated red light signal transduction of plant phytochrome B.</name><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&lt;sup>Y276H&lt;/sup>‒PIF6 complex, and the truncated phyBN&lt;sup>Y276H&lt;/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</description><dates><release>2025-01-01T00:00:00Z</release><publication>2025 May</publication><modification>2026-06-02T20:46:27.171Z</modification><creation>2026-04-20T03:10:59.442Z</creation></dates><accession>S-EPMC12098889</accession><cross_references><pubmed>40404641</pubmed><doi>10.1038/s41421-025-00802-3</doi></cross_references></HashMap>