Structural insight into brassinosteroid perception by BRI1open access
- Authors
- She, Ji; Han, Zhifu; Kim, Tae Wuk; Wang, Jinjing; Cheng, Wei; Chang, Junbiao; Shi, Shuai; Wang, Jiawei; Yang, Maojun; Wang, Zhi-Yong; Chai, Jijie
- Issue Date
- Jun-2011
- Publisher
- Nature Publishing Group
- Citation
- Nature, v.474, no.7352, pp.472 - 477
- Indexed
- SCIE
SCOPUS
- Journal Title
- Nature
- Volume
- 474
- Number
- 7352
- Start Page
- 472
- End Page
- 477
- URI
- https://scholarworks.bwise.kr/hanyang/handle/2021.sw.hanyang/168165
- DOI
- 10.1038/nature10178
- ISSN
- 0028-0836
- 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.
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