4LSA

Crystal structure of BRI1 sud1 (Gly643Glu) bound to brassinolide

Summary for 4LSA

• Entry DOI: 10.2210/pdb4lsa/pdb
• Related: 3RIZ 3RJ0 4LSC 4LSX
• Descriptor: Protein BRASSINOSTEROID INSENSITIVE 1, alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• Functional Keywords: lrr-domain, membrane receptor, brassinosteroid binding, n-glycosylation, protein binding, steroid binding protein
• Biological source: Arabidopsis thaliana (mouse-ear cress)
• Cellular location: Cell membrane; Single-pass type I membrane protein: O22476
• Total number of polymer chains: 1
• Total formula weight: 87338.15

Authors

Santiago, J.,Henzler, C.,Hothorn, M. (deposition date: 2013-07-22, release date: 2013-09-04, Last modification date: 2024-11-06)

Primary citation

Santiago, J.,Henzler, C.,Hothorn, M.
Molecular mechanism for plant steroid receptor activation by somatic embryogenesis co-receptor kinases.
Science, 341:889-892, 2013

PubMed Abstract: Brassinosteroids, which control plant growth and development, are sensed by the leucine-rich repeat (LRR) domain of the membrane receptor kinase BRASSINOSTEROID INSENSITIVE 1 (BRI1), but it is unknown how steroid binding at the cell surface activates the cytoplasmic kinase domain of the receptor. A family of somatic embryogenesis receptor kinases (SERKs) has been genetically implicated in mediating early brassinosteroid signaling events. We found a direct and steroid-dependent interaction between the BRI1 and SERK1 LRR domains by analysis of their complex crystal structure at 3.3 angstrom resolution. We show that the SERK1 LRR domain is involved in steroid sensing and, through receptor-co-receptor heteromerization, in the activation of the BRI1 signaling pathway. Our work reveals how known missense mutations in BRI1 and in SERKs modulate brassinosteroid signaling and the targeting mechanism of BRI1 receptor antagonists.

PubMed: 23929946
DOI: 10.1126/science.1242468

Experimental method

X-RAY DIFFRACTION (2.5 Å)