6S6Q

Crystal structure of the LRR ectodomain of the plant membrane receptor kinase GASSHO1/SCHENGEN3 from Arabidopsis thaliana in complex with CASPARIAN STRIP INTEGRITY FACTOR 2.

Summary for 6S6Q

• Entry DOI: 10.2210/pdb6s6q/pdb
• Descriptor: LRR receptor-like serine/threonine-protein kinase GSO1, Protein CASPARIAN STRIP INTEGRITY FACTOR 2, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• Functional Keywords: membrane receptor kinase, leucine-rich repeat domain, peptide hormone identification, casparian strip, root development, receptor activation, signaling protein
• Biological source: Arabidopsis thaliana (Mouse-ear cress); More
• Total number of polymer chains: 4
• Total formula weight: 200985.19

Authors

Okuda, S.,Moretti, A.,Hothorn, M. (deposition date: 2019-07-03, release date: 2020-01-29, Last modification date: 2024-01-24)

Primary citation

Okuda, S.,Fujita, S.,Moretti, A.,Hohmann, U.,Doblas, V.G.,Ma, Y.,Pfister, A.,Brandt, B.,Geldner, N.,Hothorn, M.
Molecular mechanism for the recognition of sequence-divergent CIF peptides by the plant receptor kinases GSO1/SGN3 and GSO2.
Proc.Natl.Acad.Sci.USA, 117:2693-2703, 2020

PubMed Abstract: Plants use leucine-rich repeat receptor kinases (LRR-RKs) to sense sequence diverse peptide hormones at the cell surface. A 3.0-Å crystal structure of the LRR-RK GSO1/SGN3 regulating Casparian strip formation in the endodermis reveals a large spiral-shaped ectodomain. The domain provides a binding platform for 21 amino acid CIF peptide ligands, which are tyrosine sulfated by the tyrosylprotein sulfotransferase TPST/SGN2. GSO1/SGN3 harbors a binding pocket for sulfotyrosine and makes extended backbone interactions with CIF2. Quantitative biochemical comparisons reveal that GSO1/SGN3-CIF2 represents one of the strongest receptor-ligand pairs known in plants. Multiple missense mutations are required to block CIF2 binding in vitro and GSO1/SGN3 function in vivo. Using structure-guided sequence analysis we uncover previously uncharacterized CIF peptides conserved among higher plants. Quantitative binding assays with known and novel CIFs suggest that the homologous LRR-RKs GSO1/SGN3 and GSO2 have evolved unique peptide binding properties to control different developmental processes. A quantitative biochemical interaction screen, a CIF peptide antagonist and genetic analyses together implicate SERK proteins as essential coreceptor kinases required for GSO1/SGN3 and GSO2 receptor activation. Our work provides a mechanistic framework for the recognition of sequence-divergent peptide hormones in plants.

PubMed: 31964818
DOI: 10.1073/pnas.1911553117

Experimental method

X-RAY DIFFRACTION (2.95 Å)