Structural basis for flg22-induced activation of the Arabidopsis FLS2-BAK1 immune complex

Yadong Sun, Lei Li, Alberto P. Macho, Zhifu Han, Zehan Hu, Cyril Zipfel, Jian Min Zhou, Jijie Chai

Research output: Contribution to journalArticle

336 Scopus citations

Abstract

Flagellin perception in Arabidopsis is through recognition of its highly conserved N-terminal epitope (flg22) by flagellin-sensitive 2 (FLS2). Flg22 binding induces FLS2 heteromerization with BRASSINOSTEROID INSENSITIVE 1-associated kinase 1 (BAK1) and their reciprocal activation followed by plant immunity. Here, we report the crystal structure of FLS2 and BAK1 ectodomains complexed with flg22 at 3.06 angstroms. A conserved and a nonconserved site from the inner surface of the FLS2 solenoid recognize the C- and N-terminal segment of flg22, respectively, without oligomerization or conformational changes in the FLS2 ectodomain. Besides directly interacting with FLS2, BAK1 acts as a co-receptor by recognizing the C terminus of the FLS2-bound flg22. Our data reveal the molecular mechanisms underlying FLS2-BAK1 complex recognition of flg22 and provide insight into the immune receptor complex activation.

Original languageEnglish (US)
Pages (from-to)624-628
Number of pages5
JournalScience
Volume342
Issue number6158
DOIs
StatePublished - Jan 1 2013
Externally publishedYes

ASJC Scopus subject areas

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    Sun, Y., Li, L., Macho, A. P., Han, Z., Hu, Z., Zipfel, C., Zhou, J. M., & Chai, J. (2013). Structural basis for flg22-induced activation of the Arabidopsis FLS2-BAK1 immune complex. Science, 342(6158), 624-628. https://doi.org/10.1126/science.1243825