8IF6
Conformational Dynamics of the D53-D3-D14 Complex in Strigolactone Signaling
This is a non-PDB format compatible entry.
Summary for 8IF6
| Entry DOI | 10.2210/pdb8if6/pdb |
| EMDB information | 35402 |
| Descriptor | F-box/LRR-repeat MAX2 homolog, Strigolactone esterase D14, SKP1-like protein 20 (3 entities in total) |
| Functional Keywords | d14 d3 d53 sl, plant protein |
| Biological source | Oryza sativa subsp. japonica (Rice) More |
| Total number of polymer chains | 3 |
| Total formula weight | 132071.33 |
| Authors | |
| Primary citation | Liu, S.,Wang, J.,Song, B.,Gong, X.,Liu, H.,Hu, Q.,Zhang, J.,Li, Q.,Zheng, J.,Wang, H.,Xu, H.E.,Li, J.,Wang, B. Conformational Dynamics of the D53-D3-D14 Complex in Strigolactone Signaling. Plant Cell.Physiol., 64:1046-1056, 2023 Cited by PubMed Abstract: Strigolactones (SLs) play fundamental roles in regulating plant architecture, which is a major factor determining crop yield. The perception and signal transduction of SLs require the formation of a complex containing the receptor DWARF14 (D14), an F-box protein D3 and a transcriptional regulator D53 in an SL-dependent manner. Structural and biochemical analyses of D14 and its orthologs DAD2 and AtD14, D3 and the complexes of ASK1-D3-AtD14 and D3CTH-D14 have made great contributions to understanding the mechanisms of SL perception. However, structural analyses of D53 and the D53-D3-D14 holo-complex are challenging, and the biochemical mechanism underlying the complex assembly remains poorly understood. Here, we found that apo-D53 was rather flexible and reconstituted the holo-complex containing D53, S-phase kinase-associated protein 1 (SKP1), D3 and D14 with rac-GR24. The cryo-electron microscopy (cryo-EM) structure of SKP1-D3-D14 in the presence of D53 was analyzed and superimposed on the crystal structure of ASK1-D3-AtD14 without D53. No large conformational rearrangement was observed, but a 9Å rotation appeared between D14 and AtD14. Using hydrogen-deuterium exchange monitored by mass spectrometry, we analyzed dynamic motifs of D14, D3 and D53 in the D53-SKP1-D3-D14 complex assembly process and further identified two potential interfaces in D53 that are located in the N and D2 domains, respectively. Together, our results uncovered the dynamic conformational changes and built a model of the holo-complex D53-SKP1-D3-D14, offering valuable information for the biochemical and genetic mechanisms of SL perception and signal transduction. PubMed: 37384578DOI: 10.1093/pcp/pcad067 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (7.09 Å) |
Structure validation
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