3RGX
Structural insight into brassinosteroid perception by BRI1
Summary for 3RGX
| Entry DOI | 10.2210/pdb3rgx/pdb |
| Related | 3RGZ |
| Related PRD ID | PRD_900017 |
| Descriptor | Protein BRASSINOSTEROID INSENSITIVE 1, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total) |
| Functional Keywords | brassinosteroid-insensitive 1 (bri1), leucine-rich repeat receptor-like kinases, leucine-rich repeat, brassinosteroid, transferase, phytohormone |
| Biological source | Arabidopsis thaliana (mouse-ear cress,thale-cress) |
| Cellular location | Cell membrane; Single-pass type I membrane protein: O22476 |
| Total number of polymer chains | 1 |
| Total formula weight | 86531.10 |
| Authors | |
| Primary citation | She, J.,Han, Z.,Kim, T.W.,Wang, J.,Cheng, W.,Chang, J.,Shi, S.,Wang, J.,Yang, M.,Wang, Z.Y.,Chai, J. Structural insight into brassinosteroid perception by BRI1. Nature, 474:472-476, 2011 Cited by PubMed Abstract: Brassinosteroids are essential phytohormones that have crucial roles in plant growth and development. Perception of brassinosteroids requires an active complex of BRASSINOSTEROID-INSENSITIVE 1 (BRI1) and BRI1-ASSOCIATED KINASE 1 (BAK1). Recognized by the extracellular leucine-rich repeat (LRR) domain of BRI1, brassinosteroids induce a phosphorylation-mediated cascade to regulate gene expression. Here we present the crystal structures of BRI1(LRR) in free and brassinolide-bound forms. BRI1(LRR) exists as a monomer in crystals and solution independent of brassinolide. It comprises a helical solenoid structure that accommodates a separate insertion domain at its concave surface. Sandwiched between them, brassinolide binds to a hydrophobicity-dominating surface groove on BRI1(LRR). Brassinolide recognition by BRI1(LRR) is through an induced-fit mechanism involving stabilization of two interdomain loops that creates a pronounced non-polar surface groove for the hormone binding. Together, our results define the molecular mechanisms by which BRI1 recognizes brassinosteroids and provide insight into brassinosteroid-induced BRI1 activation. PubMed: 21666666DOI: 10.1038/nature10178 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.47 Å) |
Structure validation
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