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Structural insight into brassinosteroid perception by BRI1

JI SHE ; ZHIFU HAN ; JIJIE CHAI ; KIM, Tae-Wuk ; JINJING WANG ; WEI CHENG ; JUNBIAO CHANG ; SHUAI SHI ; JIAWEI WANG ; MAOJUN YANG ; WANG, Zhi-Yong

Nature (London), 2011-06, Vol.474 (7352), p.472-476 [Periódico revisado por pares]

London: Nature Publishing Group

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Título:
Structural insight into brassinosteroid perception by BRI1
Autor: JI SHE ; ZHIFU HAN ; JIJIE CHAI ; KIM, Tae-Wuk ; JINJING WANG ; WEI CHENG ; JUNBIAO CHANG ; SHUAI SHI ; JIAWEI WANG ; MAOJUN YANG ; WANG, Zhi-Yong
Assuntos: 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
É parte de: Nature (London), 2011-06, Vol.474 (7352), p.472-476
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
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These authors contributed equally to this work
Descrição: 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.
Editor: London: Nature Publishing Group
Idioma: Inglês

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Structural insight into brassinosteroid perception by BRI1

JI SHE ; ZHIFU HAN ; JIJIE CHAI ; KIM, Tae-Wuk ; JINJING WANG ; WEI CHENG ; JUNBIAO CHANG ; SHUAI SHI ; JIAWEI WANG ; MAOJUN YANG ; WANG, Zhi-Yong

London: Nature Publishing Group

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