Structural insight into brassinosteroid perception by BRI1.

Structural insight into brassinosteroid perception by BRI1.
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DOI:
10.1038/nature10178
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发表时间:
2011-06-12
期刊:
影响因子:
64.8
通讯作者:
Chai, Jijie
Chai, Jijie
中科院分区:
综合性期刊1区
文献类型:
--
作者:
She, Ji;Han, Zhifu;Kim, Tae-Wuk;Wang, Jinjing;Cheng, Wei;Chang, Junbiao;Shi, Shuai;Wang, Jiawei;Yang, Maojun;Wang, Zhi-Yong;Chai, Jijie

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油菜素内酯(BR)是必需的植物激素,在植物生长和发育中发挥着至关重要的作用。 BR 的感知需要油菜素类固醇不敏感 1 (BRI1) 和 BRI1 相关激酶 1 (BAK1) 的活性复合物。 BR 被 BRI1 的胞外富含亮氨酸重复序列 (LRR) 结构域识别,诱导磷酸化介导的级联反应来调节基因表达。在这里,我们展示了游离形式和油菜素内酯 (BL) 结合形式的 BRI1-LRR 的晶体结构。 BRI1-LRR 作为单体存在于晶体和溶液中,独立于 BL。它包括一个螺旋螺线管结构,该结构在其凹面处容纳一个单独的插入域。 BL 夹在它们之间,与 BRI1-LRR 上疏水性主导的表面凹槽结合。 BRI1-LRR 的 BL 识别是通过诱导拟合机制实现的,该机制涉及两个域间环的稳定,从而为激素结合创建明显的非极性表面凹槽。总之,我们的结果定义了 BRI1 识别 BR 的分子机制,并提供了对 BR 诱导的 BRI1 激活的深入了解。
Brassinosteroids (BRs) are essential phytohormones that play crucial roles in plant growth and development. Perception of BRs 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, BRs induce a phosphorylation-mediated cascade to regulate gene expression. Here we present the crystal structures of BRI1-LRR in free and brassinolide (BL)-bound forms. BRI1-LRR exists as a monomer in crystals and solution independent of BL. It comprises a helical solenoid structure that accommodates a separate insertion domain at its concave surface. Sandwiched between them, BL binds to a hydrophobicity-dominating surface groove on BRI1-LRR. BL recognition by BRI1-LRR is through an induced-fit mechanism involving stabilization of two inter-domain loops that creates a pronounced non-polar surface groove for the hormone binding. Together, our results define the molecular mechanisms by which BRI1 recognizes BRs and provide insight into BR-induced BRI1 activation.
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