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| Title | A bacteriophytochrome Pr/Pfr heterodimer studied through single-particle time-resolved cryo-electron microscopy. |
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| Journal, issue, pages | Commun Chem, Year 2026 |
| Publish date | Jun 8, 2026 |
Authors | Prabin Karki / William C Budell / Rohit Kannachel / David Menendez / Carolina Hernandez / Joshua H Mendez / Shemiran Kanou / Manjeet Singh / Chavdar Slavov / Peter Schwander / Tek Narsingh Malla / Emina A Stojković / Marius Schmidt / ![]() |
| PubMed Abstract | Phytochromes are dimeric photoreceptors found in bacteria, fungi, and plants that reversibly interconvert between a red-absorbing Pr state and a far-red-absorbing Pfr state. In bacteria, phytochromes ...Phytochromes are dimeric photoreceptors found in bacteria, fungi, and plants that reversibly interconvert between a red-absorbing Pr state and a far-red-absorbing Pfr state. In bacteria, phytochromes (BphPs) regulate diverse responses through a two-component signaling pathway comprising a C-terminal histidine kinase (HK) and a response regulator. A previous cryo-EM study of the wild-type BphP from Stigmatella aurantiaca (SaBphP2) revealed a stable Pr/Pfr heterodimer in which the two protomers adopt distinct Pr and Pfr conformations. Here, using the Spotiton technique, we captured the same heterodimer by illuminating SaBphP2 particles on the cryo-EM grid and vitrifying them 10 ms later. Comparison with the Pr/Pr homodimer reveals a 180° rotation of the HK domain, driven by an unwinding of the coiled-coil helices that connect the photosensory core to the enzymatic domain. The large-scale reorientations provide mechanistic insight into light-triggered signal transduction mediated by bacterial phytochromes. |
External links | Commun Chem / PubMed:42260277 |
| Methods | EM (single particle) |
| Resolution | 5.01 - 5.85 Å |
| Structure data | EMDB-73380, PDB-9ys3: EMDB-73612, PDB-9yxn: |
| Chemicals | ![]() ChemComp-BLA: |
| Source |
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Keywords | SIGNALING PROTEIN / Signal Transduction / Photoactivation |
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stigmatella aurantiaca (bacteria)
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