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.

spinqualitylabelsall models 6s6q, resolution 2.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6s6q is a 4 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.95Å Ligands: BMA, NAG, TYS Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GSO1_ARATH Together with GSO2, receptor-like serine/threonine-kinase required during the development of the epidermal surface in embryos and cotyledons (PubMed:18088309). In coordination with GSO2, regulates root growth through control of cell division and cell fate specification. Controls seedling root growth by modulating sucrose response after germination (PubMed:24123341). Receptor of the peptide hormones CIF1 and CIF2 required for contiguous Casparian strip diffusion barrier formation in roots (PubMed:28104889). Required for localizing CASP proteins into the Casparian strip following an uninterrupted, ring-like domain, to trigger endodermal differentiation and thus regulate potassium ion (K) homeostasis. Involved in the maintenance of water transport and root pressure. May also be involved in the regulation of suberin accumulation in the endodermis (PubMed:25233277). Publication Abstract from PubMed Plants use leucine-rich repeat receptor kinases (LRR-RKs) to sense sequence diverse peptide hormones at the cell surface. A 3.0-A 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. Molecular mechanism for the recognition of sequence-divergent CIF peptides by the plant receptor kinases GSO1/SGN3 and GSO2.,Okuda S, Fujita S, Moretti A, Hohmann U, Doblas VG, Ma Y, Pfister A, Brandt B, Geldner N, Hothorn M Proc Natl Acad Sci U S A. 2020 Feb 4;117(5):2693-2703. doi:, 10.1073/pnas.1911553117. Epub 2020 Jan 21. PMID:31964818 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Serine/threonine protein kinase 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA