Structural insight into brassinosteroid perception by BRI1

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) domai...

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Bibliographic Details
Published in:Nature (London) 2011-06, Vol.474 (7352), p.472-476
Main Authors: JI SHE, ZHIFU HAN, JIJIE CHAI, KIM, Tae-Wuk, JINJING WANG, WEI CHENG, JUNBIAO CHANG, SHUAI SHI, JIAWEI WANG, MAOJUN YANG, WANG, Zhi-Yong
Format: Article
Language:English
Subjects:
Agronomy. Soil science and plant productions
Analysis
Arabidopsis
Arabidopsis - chemistry
Arabidopsis - metabolism
Arabidopsis Proteins - chemistry
Arabidopsis Proteins - metabolism
Binding Sites
Biological and medical sciences
Brassinosteroids
Cell receptors
Cholestanols - chemistry
Cholestanols - metabolism
Crystallography, X-Ray
Economic plant physiology
Enzyme Activation
Fundamental and applied biological sciences. Psychology
Genetic aspects
Genetics and breeding of economic plants
Growth and development
Growth regulators
Hydrophobic and Hydrophilic Interactions
Kinases
Models, Molecular
Phosphorylation
Plant hormones
Protein Binding
Protein Folding
Protein Kinases - chemistry
Protein Kinases - metabolism
Protein Structure, Tertiary
Proteins
Steroids, Heterocyclic - chemistry
Steroids, Heterocyclic - metabolism
Structure
Structure-Activity Relationship
Substrate Specificity
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Summary: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.
ISSN:0028-0836
1476-4687
DOI:10.1038/nature10178