5B3H
The crystal structure of the JACKDAW/IDD10 bound to the heterodimeric SHR-SCR complex
Summary for 5B3H
Entry DOI | 10.2210/pdb5b3h/pdb |
Related | 5B3G |
Descriptor | Protein SCARECROW, Protein SHORT-ROOT, Zinc finger protein JACKDAW, ... (5 entities in total) |
Functional Keywords | transcription factor, transcription |
Biological source | Arabidopsis thaliana (Mouse-ear cress) More |
Total number of polymer chains | 6 |
Total formula weight | 195245.88 |
Authors | Hirano, Y.,Suyama, T.,Nakagawa, M.,Hakoshima, T. (deposition date: 2016-02-29, release date: 2017-03-01, Last modification date: 2023-11-08) |
Primary citation | Hirano, Y.,Nakagawa, M.,Suyama, T.,Murase, K.,Shirakawa, M.,Takayama, S.,Sun, T.P.,Hakoshima, T. Structure of the SHR-SCR heterodimer bound to the BIRD/IDD transcriptional factor JKD Nat Plants, 3:17010-17010, 2017 Cited by PubMed Abstract: The plant-specific GAI, RGA and SCR (GRAS) family proteins play critical roles in plant development and signalling. Two GRAS proteins, SHORT-ROOT (SHR) and SCARECROW (SCR), cooperatively direct asymmetric cell division and the patterning of root cell types by transcriptional control in conjunction with BIRD/INDETERMINATE DOMAIN (IDD) transcription factors, although precise details of these specific interactions and actions remain unknown. Here, we present the crystal structures of the SHR-SCR binary and JACKDAW (JKD)/IDD10-SHR-SCR ternary complexes. Each GRAS domain comprises one α/β core subdomain with an α-helical cap that mediates heterodimerization by forming an intermolecular helix bundle. The α/β core subdomain of SHR forms the BIRD binding groove, which specifically recognizes the zinc fingers of JKD. We identified a conserved SHR-binding motif in 13 BIRD/IDD transcription factors. Our results establish a structural basis for GRAS-GRAS and GRAS-BIRD interactions and provide valuable clues towards our understanding of these regulators, which are involved in plant-specific signalling networks. PubMed: 28211915DOI: 10.1038/nplants.2017.10 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
Download full validation report