4MN8

Crystal structure of flg22 in complex with the FLS2 and BAK1 ectodomains

Summary for 4MN8

• Entry DOI: 10.2210/pdb4mn8/pdb
• Related: 4MNA
• Descriptor: LRR receptor-like serine/threonine-protein kinase FLS2, BRASSINOSTEROID INSENSITIVE 1-associated receptor kinase 1, flg22, ... (6 entities in total)
• Functional Keywords: fls2, bak1, flg22, flagellin, plant immunity, leucine-rich repeat, transferase-transferase receptor complex, transferase/transferase receptor
• Biological source: Arabidopsis thaliana (mouse-ear cress,thale-cress); More
• Total number of polymer chains: 3
• Total formula weight: 116383.23

Authors

Chai, J.,Sun, Y.,Han, Z. (deposition date: 2013-09-10, release date: 2013-12-04, Last modification date: 2023-11-08)

Primary citation

Sun, Y.,Li, L.,Macho, A.P.,Han, Z.,Hu, Z.,Zipfel, C.,Zhou, J.M.,Chai, J.
Structural basis for flg22-induced activation of the Arabidopsis FLS2-BAK1 immune complex.
Science, 342:624-628, 2013

PubMed 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.

PubMed: 24114786
DOI: 10.1126/science.1243825

Experimental method

X-RAY DIFFRACTION (3.062 Å)