9MB8
the complex of D14 and RGSV P3
Summary for 9MB8
| Entry DOI | 10.2210/pdb9mb8/pdb |
| EMDB information | 63769 |
| Descriptor | Strigolactone esterase D14, p3 (2 entities in total) |
| Functional Keywords | dawrf14, plant protein |
| Biological source | Oryza sativa Japonica Group (Japanese rice) More |
| Total number of polymer chains | 4 |
| Total formula weight | 105448.70 |
| Authors | Huang, Y.C. (deposition date: 2025-03-15, release date: 2026-03-04, Last modification date: 2026-04-29) |
| Primary citation | Yang, G.,Wu, M.,Zhang, S.,Huang, Y.,Liu, Y.,Yu, X.,Hu, J.,Mi, L.,Gan, P.,Wu, Y.,Zou, J.,Zhang, B.,Hu, Q.,Hu, J.,Yao, R.,Zhong, B.,Huang, X.,Xie, H.,Ji, Y.,Li, Y.,Zhang, J.,Yan, L.,Ding, S.W.,Zhao, S.,Wu, J. Editing strigolactone hormone receptor for robust antiviral silencing in rice. Cell, 189:2054-, 2026 Cited by PubMed Abstract: The small interfering RNA (siRNA) pathway directs broad-spectrum antiviral defense through RNA silencing so that virulent infection requires efficient suppression of the defense mechanism. Here, we show that strigolactone (SL) hormone signaling promotes antiviral silencing in rice plants by transcriptional activation of RNA-dependent RNA polymerase 1 (RDR1) and RDR6. We demonstrate that protein P3 of the rice grassy stunt virus (RGSV) blocks SL signaling by directly sequestering the receptor DWARF14 from DWARF3. Structural and functional analyses of the P3-DWARF14 complex reveal that the aspartic acid at position 102 (D102) of DWARF14 is essential for the P3 interaction but not for SL perception. Notably, a single D102N substitution of DWARF14, introduced into two rice cultivars by cytosine base editing (CBE) confers resistance against RGSV by blocking viral suppression of SL signaling-dependent antiviral silencing. Our findings establish a transgene-free strategy for engineering disease resistance by precise genome editing of the SL receptor to escape pathogen suppression of the endogenous defense pathway. PubMed: 41742412DOI: 10.1016/j.cell.2026.01.013 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.67 Å) |
Structure validation
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