Structural insight into brassinosteroid perception by BRI1

Ji She, Zhifu Han, Tae-Wuk Kim, Jinjing Wang, Wei Cheng, Junbiao Chang, Shuai Shi, Jiawei Wang, Maojun Yang, Zhi-Yong Wang and Jijie Chai ()
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Ji She: Key Laboratory for Protein Sciences of Ministry of Education School of Life Sciences, Tsinghua University
Zhifu Han: Key Laboratory for Protein Sciences of Ministry of Education School of Life Sciences, Tsinghua University
Tae-Wuk Kim: Carnegie Institution for Science
Jinjing Wang: National Institute of Biological Sciences, No. 7 Science Park Road, Beijing 102206, China
Wei Cheng: National Institute of Biological Sciences, No. 7 Science Park Road, Beijing 102206, China
Junbiao Chang: Zhengzhou University
Shuai Shi: Zhengzhou University
Jiawei Wang: Key Laboratory for Protein Sciences of Ministry of Education School of Life Sciences, Tsinghua University
Maojun Yang: Key Laboratory for Protein Sciences of Ministry of Education School of Life Sciences, Tsinghua University
Zhi-Yong Wang: Carnegie Institution for Science
Jijie Chai: Key Laboratory for Protein Sciences of Ministry of Education School of Life Sciences, Tsinghua University

Nature, 2011, vol. 474, issue 7352, 472-476

Abstract: 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.

Date: 2011
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DOI: 10.1038/nature10178

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