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9LUO

Cryo-EM structure of Arabidopsis thaliana RGA in complex with GID1A, SLY1, and ASK2 (focused map)

Summary for 9LUO
Entry DOI10.2210/pdb9luo/pdb
EMDB information63400
DescriptorDELLA protein RGA, F-box protein GID2, SKP1-like protein 1B (3 entities in total)
Functional Keywordsgibberellin, della motif, gras domain, plant growth, hormone
Biological sourceArabidopsis thaliana (thale cress)
More
Total number of polymer chains3
Total formula weight100990.81
Authors
Islam, S.,Park, K.,Kwon, E.,Kim, D.Y. (deposition date: 2025-02-09, release date: 2025-07-09, Last modification date: 2025-07-23)
Primary citationIslam, S.,Park, K.,Xia, J.,Kwon, E.,Kim, D.Y.
Structural insights into gibberellin-mediated DELLA protein degradation.
Mol Plant, 18:1210-1221, 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: 40542507
DOI: 10.1016/j.molp.2025.06.010
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.07 Å)
Structure validation

240971

건을2025-08-27부터공개중

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