6TOC
Crystal structure of the oligomerisation domain of the transcription factor PHOSPHATE STARVATION RESPONSE 1 from Arabidopsis (crystal form 3).
This is a non-PDB format compatible entry.
Summary for 6TOC
| Entry DOI | 10.2210/pdb6toc/pdb |
| Related | 6TO5 6TO9 |
| Descriptor | Protein PHOSPHATE STARVATION RESPONSE 1 (2 entities in total) |
| Functional Keywords | phosphate starvation, myb domain, coiled-coil domain, inositol pyrophosphate, plant nutrition, transcription |
| Biological source | Arabidopsis thaliana (thale cress) |
| Total number of polymer chains | 2 |
| Total formula weight | 18745.40 |
| Authors | Hothorn, M. (deposition date: 2019-12-11, release date: 2021-01-13, Last modification date: 2024-01-24) |
| Primary citation | Ried, M.K.,Wild, R.,Zhu, J.,Pipercevic, J.,Sturm, K.,Broger, L.,Harmel, R.K.,Abriata, L.A.,Hothorn, L.A.,Fiedler, D.,Hiller, S.,Hothorn, M. Inositol pyrophosphates promote the interaction of SPX domains with the coiled-coil motif of PHR transcription factors to regulate plant phosphate homeostasis. Nat Commun, 12:384-384, 2021 Cited by PubMed Abstract: Phosphorus is an essential nutrient taken up by organisms in the form of inorganic phosphate (Pi). Eukaryotes have evolved sophisticated Pi sensing and signaling cascades, enabling them to stably maintain cellular Pi concentrations. Pi homeostasis is regulated by inositol pyrophosphate signaling molecules (PP-InsPs), which are sensed by SPX domain-containing proteins. In plants, PP-InsP-bound SPX receptors inactivate Myb coiled-coil (MYB-CC) Pi starvation response transcription factors (PHRs) by an unknown mechanism. Here we report that a InsP-SPX complex targets the plant-unique CC domain of PHRs. Crystal structures of the CC domain reveal an unusual four-stranded anti-parallel arrangement. Interface mutations in the CC domain yield monomeric PHR1, which is no longer able to bind DNA with high affinity. Mutation of conserved basic residues located at the surface of the CC domain disrupt interaction with the SPX receptor in vitro and in planta, resulting in constitutive Pi starvation responses. Together, our findings suggest that InsP regulates plant Pi homeostasis by controlling the oligomeric state and hence the promoter binding capability of PHRs via their SPX receptors. PubMed: 33452263DOI: 10.1038/s41467-020-20681-4 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.853 Å) |
Structure validation
Download full validation report
