9LUM
Cryo-EM structure of Arabidopsis thaliana RGA in complex with GID1A
Summary for 9LUM
| Entry DOI | 10.2210/pdb9lum/pdb |
| EMDB information | 63398 |
| Descriptor | DELLA protein RGA, Gibberellin receptor GID1A, GIBBERELLIN A3, ... (4 entities in total) |
| Functional Keywords | gibberellin, della motif, gras domain, plant growth, hormone |
| Biological source | Arabidopsis thaliana (thale cress) More |
| Total number of polymer chains | 2 |
| Total formula weight | 103268.42 |
| Authors | |
| Primary citation | Islam, S.,Park, K.,Xia, J.,Kwon, E.,Kim, D.Y. Structural insights of gibberellin-mediated DELLA protein degradation. Mol Plant, 2025 Cited by PubMed Abstract: Gibberellin promotes plant growth by downregulating DELLA proteins, which act as growth repressors. In the presence of gibberellin, the gibberellin receptor GID1 binds DELLA proteins, triggering their degradation through polyubiquitination by the SCF ubiquitin E3 ligase. Despite extensive studies, the molecular mechanisms by which DELLA proteins assemble with SCF to regulate plant growth remain poorly understood. Here, we present two cryo-electron microscopy structures of the Arabidopsis thaliana DELLA protein RGA in complex with GID1A and GID1A-SLY1-ASK2, respectively. Structural analyses revealed that RGA interacts with GID1A and SLY1 through nonoverlapping binding surfaces, stabilizing the proteins. This suggests that the SCF-RGA-GID1A complex assembles through a stepwise stabilization process induced by gibberellin. Furthermore, structural comparison with GRAS proteins indicates that RGA does not interact with IDD-family transcription factors when bound to SLY1, suggesting that DELLA protein binding to GID1/SLY1 and to transcription factors is mutually exclusive. These findings provide new insights into the gibberellin-mediated regulation of transcription factor activity by DELLA proteins. PubMed: 40542507DOI: 10.1016/j.molp.2025.06.010 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.66 Å) |
Structure validation
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