3RGZ

Structural insight into brassinosteroid perception by BRI1

Summary for 3RGZ

• Entry DOI: 10.2210/pdb3rgz/pdb
• Related: 3RGX
• 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, ... (8 entities in total)
• Functional Keywords: phytohormone, brassinosteroid-insensitive 1, leucine-rich repeat receptor-like kinases, leucine-rich repeat, brassinosteroid, transferase
• 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: 87107.84

Authors

Chai, J.,Han, Z.,She, J.,Wang, J.,Cheng, W. (deposition date: 2011-04-11, release date: 2011-06-15, Last modification date: 2024-10-09)

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

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: 21666666
DOI: 10.1038/nature10178

Experimental method

X-RAY DIFFRACTION (2.281 Å)