spacer
spacer

PDBsum entry 4mn8

Go to PDB code: 
Top Page protein ligands Protein-protein interface(s) links
Transferase/transferase receptor PDB id
4mn8
Contents
Protein chains
759 a.a.
175 a.a.
21 a.a.
Ligands
NAG-NAG
NAG ×9
SO4 ×16

References listed in PDB file
Key reference
Title Structural basis for flg22-Induced activation of the arabidopsis fls2-Bak1 immune complex.
Authors Y.Sun, L.Li, A.P.Macho, Z.Han, Z.Hu, C.Zipfel, J.M.Zhou, J.Chai.
Ref. Science, 2013, 342, 624-628. [DOI no: 10.1126/science.1243825]
PubMed id 24114786
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.
PROCHECK
Go to PROCHECK summary
 Headers

 

spacer

spacer