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9IRK

Cryo-EM structure of PhyB(Y276H,1-908)-PIF6beta complex

Summary for 9IRK
Entry DOI10.2210/pdb9irk/pdb
EMDB information60816
DescriptorPhytochrome B, Transcription factor PIF6, 3-[5-[[(3~{R},4~{R})-3-ethyl-4-methyl-5-oxidanylidene-3,4-dihydropyrrol-2-yl]methyl]-2-[[5-[(4-ethyl-3-methyl-5-oxidanylidene-pyrrol-2-yl)methyl]-3-(3-hydroxy-3-oxopropyl)-4-methyl-1~{H}-pyrrol-2-yl]methyl]-4-methyl-1~{H}-pyrrol-3-yl]propanoic acid (3 entities in total)
Functional Keywordspif6-mediated, red light, signal transduction, phytochrome b, gene regulation
Biological sourceArabidopsis thaliana (thale cress)
More
Total number of polymer chains3
Total formula weight220085.77
Authors
Jia, H.L.,Guan, Z.Y.,Ding, J.Y.,Wang, X.Y.,Ma, L.,Yin, P. (deposition date: 2024-07-16, release date: 2025-06-04)
Primary citationJia, H.,Guan, Z.,Ding, J.,Wang, X.,Tian, D.,Zhu, Y.,Zhang, D.,Liu, Z.,Ma, L.,Yin, P.
Structural insight into PIF6-mediated red light signal transduction of plant phytochrome B.
Cell Discov, 11:51-51, 2025
Cited by
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‒PIF6 complex, and the truncated phyBN‒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 photosensory modules. The interaction between phyB-Pfr and PIF6 influences the dimerization and transcriptional activation activity of PIF6, and PIF6 stabilizes the N-terminal extension of phyB-Pfr and increases the Pr→Pfr photoconversion efficiency of phyB. Our findings reveal the molecular mechanisms underlying Pr→Pfr photoconversion and PIF6-mediated red light signal transduction of phyB.
PubMed: 40404641
DOI: 10.1038/s41421-025-00802-3
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.8 Å)
Structure validation

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