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

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.

DOI: 10.1126/science.1243825

1 Figure or Table

05010020132014201520162017
Citations per Year

287 Citations

Semantic Scholar estimates that this publication has 287 citations based on the available data.

See our FAQ for additional information.

Cite this paper

@article{Sun2013StructuralBF, title={Structural basis for flg22-induced activation of the Arabidopsis FLS2-BAK1 immune complex.}, author={Yadong Sun and Lei Li and Alberto P Macho and Zhifu Han and Zehan Hu and Cyril Zipfel and Jian-Min Zhou and Jijie Chai}, journal={Science}, year={2013}, volume={342 6158}, pages={624-8} }