7NB0
Structure of the DNA-binding domain of SEPALLATA 3
Summary for 7NB0
| Entry DOI | 10.2210/pdb7nb0/pdb |
| Descriptor | Developmental protein SEPALLATA 3 (2 entities in total) |
| Functional Keywords | transcription factor, mads family, dna-binding domain, plant protein |
| Biological source | Arabidopsis thaliana (Mouse-ear cress) |
| Total number of polymer chains | 4 |
| Total formula weight | 26414.87 |
| Authors | Zubieta, C.,Nanao, M.H. (deposition date: 2021-01-25, release date: 2021-07-14, Last modification date: 2024-01-31) |
| Primary citation | Lai, X.,Vega-Leon, R.,Hugouvieux, V.,Blanc-Mathieu, R.,van der Wal, F.,Lucas, J.,Silva, C.S.,Jourdain, A.,Muino, J.M.,Nanao, M.H.,Immink, R.,Kaufmann, K.,Parcy, F.,Smaczniak, C.,Zubieta, C. The intervening domain is required for DNA-binding and functional identity of plant MADS transcription factors. Nat Commun, 12:4760-4760, 2021 Cited by PubMed Abstract: The MADS transcription factors (TF) are an ancient eukaryotic protein family. In plants, the family is divided into two main lineages. Here, we demonstrate that DNA binding in both lineages absolutely requires a short amino acid sequence C-terminal to the MADS domain (M domain) called the Intervening domain (I domain) that was previously defined only in type II lineage MADS. Structural elucidation of the MI domains from the floral regulator, SEPALLATA3 (SEP3), shows a conserved fold with the I domain acting to stabilise the M domain. Using the floral organ identity MADS TFs, SEP3, APETALA1 (AP1) and AGAMOUS (AG), domain swapping demonstrate that the I domain alters genome-wide DNA-binding specificity and dimerisation specificity. Introducing AG carrying the I domain of AP1 in the Arabidopsis ap1 mutant resulted in strong complementation and restoration of first and second whorl organs. Taken together, these data demonstrate that the I domain acts as an integral part of the DNA-binding domain and significantly contributes to the functional identity of the MADS TF. PubMed: 34362909DOI: 10.1038/s41467-021-24978-w PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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