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

Sun, Yadong, Li, Lei, Macho, Alberto P, Han, Zhifu, Hu, Zehan, Zipfel, Cyril, Zhou, Jian-Min and Chai, Jijie (2013) Structural basis for flg22-induced activation of the Arabidopsis FLS2-BAK1 immune complex. Science, 342 (6158). pp. 624-628. ISSN 0036-8075

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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.

Item Type:	Article
Uncontrolled Keywords:	antigen-antibody complex,arabidopsis,arabidopsis proteins,crystallography, x-ray,flagellin,protein kinases,protein structure, tertiary,protein-serine-threonine kinases
Faculty \ School:	Faculty of Science > School of Biological Sciences Faculty of Science > The Sainsbury Laboratory
UEA Research Groups:	Faculty of Science > Research Groups > Plant Sciences
Depositing User:	Pure Connector
Date Deposited:	04 Jul 2014 12:43
Last Modified:	24 Oct 2022 06:24
URI:	https://ueaeprints.uea.ac.uk/id/eprint/48864
DOI:	10.1126/science.1243825

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