6RYD
WUS-HD bound to TGAA DNA
Summary for 6RYD
Entry DOI | 10.2210/pdb6ryd/pdb |
Related | 6RY3 |
Descriptor | Protein WUSCHEL, DNA (5'-D(*AP*GP*TP*GP*TP*AP*TP*GP*AP*AP*TP*GP*AP*AP*CP*G)-3'), DNA (5'-D(*CP*GP*TP*TP*CP*AP*TP*TP*CP*AP*TP*AP*CP*AP*CP*T)-3'), ... (5 entities in total) |
Functional Keywords | homeodomain transcription factor, dna binding protein |
Biological source | Arabidopsis thaliana (thale cress) More |
Total number of polymer chains | 8 |
Total formula weight | 55409.87 |
Authors | Sloan, J.J.,Wild, K.,Sinning, I. (deposition date: 2019-06-10, release date: 2020-04-29, Last modification date: 2024-01-24) |
Primary citation | Sloan, J.,Hakenjos, J.P.,Gebert, M.,Ermakova, O.,Gumiero, A.,Stier, G.,Wild, K.,Sinning, I.,Lohmann, J.U. Structural basis for the complex DNA binding behavior of the plant stem cell regulator WUSCHEL. Nat Commun, 11:2223-2223, 2020 Cited by PubMed Abstract: Stem cells are one of the foundational evolutionary novelties that allowed the independent emergence of multicellularity in the plant and animal lineages. In plants, the homeodomain (HD) transcription factor WUSCHEL (WUS) is essential for the maintenance of stem cells in the shoot apical meristem. WUS has been reported to bind to diverse DNA motifs and to act as transcriptional activator and repressor. However, the mechanisms underlying this remarkable behavior have remained unclear. Here, we quantitatively delineate WUS binding to three divergent DNA motifs and resolve the relevant structural underpinnings. We show that WUS exhibits a strong binding preference for TGAA repeat sequences, while retaining the ability to weakly bind to TAAT elements. This behavior is attributable to the formation of dimers through interactions of specific residues in the HD that stabilize WUS DNA interaction. Our results provide a mechanistic basis for dissecting WUS dependent regulatory networks in plant stem cell control. PubMed: 32376862DOI: 10.1038/s41467-020-16024-y PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.575 Å) |
Structure validation
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