6FIF

Crystal structure of the BRI1 Gly644-Asp (bri1-6) mutant from Arabidopsis thaliana.

Summary for 6FIF

• Entry DOI: 10.2210/pdb6fif/pdb
• Related: 3RGX 3RGZ 3RIZ 3RJ0 4LSA 4LSX 4M7E
• Descriptor: Protein BRASSINOSTEROID INSENSITIVE 1, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total)
• Functional Keywords: leucine rich repeat receptor, membrane receptor, ectodomain, protein binding
• Biological source: Arabidopsis thaliana (thale cress)
• Cellular location: Cell membrane ; Single-pass type I membrane protein : O22476
• Total number of polymer chains: 1
• Total formula weight: 93810.22

Authors

Hothorn, M.,Santiago, J.,Hohmann, U. (deposition date: 2018-01-18, release date: 2018-01-31, Last modification date: 2024-10-23)

Primary citation

Hohmann, U.,Santiago, J.,Nicolet, J.,Olsson, V.,Spiga, F.M.,Hothorn, L.A.,Butenko, M.A.,Hothorn, M.
Mechanistic basis for the activation of plant membrane receptor kinases by SERK-family coreceptors.
Proc. Natl. Acad. Sci. U.S.A., 115:3488-3493, 2018

PubMed Abstract: Plant-unique membrane receptor kinases with leucine-rich repeat ectodomains (LRR-RKs) can sense small molecule, peptide, and protein ligands. Many LRR-RKs require SERK-family coreceptor kinases for high-affinity ligand binding and receptor activation. How one coreceptor can contribute to the specific binding of distinct ligands and activation of different LRR-RKs is poorly understood. Here we quantitatively analyze the contribution of SERK3 to ligand binding and activation of the brassinosteroid receptor BRI1 and the peptide hormone receptor HAESA. We show that while the isolated receptors sense their respective ligands with drastically different binding affinities, the SERK3 ectodomain binds the ligand-associated receptors with very similar binding kinetics. We identify residues in the SERK3 N-terminal capping domain, which allow for selective steroid and peptide hormone recognition. In contrast, residues in the SERK3 LRR core form a second, constitutive receptor-coreceptor interface. Genetic analyses of protein chimera between BRI1 and SERK3 define that signaling-competent complexes are formed by receptor-coreceptor heteromerization in planta. A functional BRI1-HAESA chimera suggests that the receptor activation mechanism is conserved among different LRR-RKs, and that their signaling specificity is encoded in the kinase domain of the receptor. Our work pinpoints the relative contributions of receptor, ligand, and coreceptor to the formation and activation of SERK-dependent LRR-RK signaling complexes regulating plant growth and development.

PubMed: 29531026
DOI: 10.1073/pnas.1714972115

Experimental method

X-RAY DIFFRACTION (2.54 Å)