4OH4
Crystal structure of BRI1 in complex with BKI1
Summary for 4OH4
| Entry DOI | 10.2210/pdb4oh4/pdb |
| Descriptor | Protein BRASSINOSTEROID INSENSITIVE 1, BRI1 kinase inhibitor 1, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (4 entities in total) |
| Functional Keywords | kinase domain, transferase, atp binding, phosphorylation, membrane, transferase-signaling protein complex, transferase/signaling protein |
| Biological source | Arabidopsis thaliana (mouse-ear cress,thale-cress) More |
| Cellular location | Cell membrane; Single-pass type I membrane protein: O22476 Cell membrane : Q9FMZ0 |
| Total number of polymer chains | 4 |
| Total formula weight | 80686.84 |
| Authors | Wang, J.,Wang, J.,Wu, J.W.,Wang, Z.X. (deposition date: 2014-01-17, release date: 2014-10-29, Last modification date: 2024-11-20) |
| Primary citation | Wang, J.,Jiang, J.,Wang, J.,Chen, L.,Fan, S.L.,Wu, J.W.,Wang, X.,Wang, Z.X. Structural insights into the negative regulation of BRI1 signaling by BRI1-interacting protein BKI1. Cell Res., 24:1328-1341, 2014 Cited by PubMed Abstract: Brassinosteroids (BRs) are essential steroid hormones that have crucial roles in plant growth and development. BRs are perceived by the cell-surface receptor-like kinase brassinosteroid insensitive 1 (BRI1). In the absence of BRs, the cytosolic kinase domain (KD) of BRI1 is inhibited by its auto-inhibitory carboxyl terminus, as well as by interacting with an inhibitor protein, BRI1 kinase inhibitor 1 (BKI1). How BR binding to the extracellular domain of BRI1 leads to activation of the KD and dissociation of BKI1 into the cytosol remains unclear. Here we report the crystal structure of BRI1 KD in complex with the interacting peptide derived from BKI1. We also provide biochemical evidence that BRI1-associated kinase 1 (BAK1) plays an essential role in initiating BR signaling. Steroid-dependent heterodimerization of BRI1 and BAK1 ectodomains brings their cytoplasmic KDs in the right orientation for competing with BKI1 and transphosphorylation. PubMed: 25331450DOI: 10.1038/cr.2014.132 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.25 Å) |
Structure validation
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