28WB
Crystal structure of the STRUBBELIG-RECEPTOR FAMILY 6 (SRF6) ectodomain from Arabidopsis thaliana
Summary for 28WB
| Entry DOI | 10.2210/pdb28wb/pdb |
| Descriptor | Protein STRUBBELIG-RECEPTOR FAMILY 6, SODIUM ION, CITRIC ACID, ... (4 entities in total) |
| Functional Keywords | receptor kinase, leucine-rich repeat domain, plant cell wall, signal transduction, membrane protein |
| Biological source | Arabidopsis thaliana (thale cress) |
| Total number of polymer chains | 1 |
| Total formula weight | 28765.68 |
| Authors | Hohmann, U.,Cargenato, A.,Hothorn, M. (deposition date: 2026-02-23, release date: 2026-03-04, Last modification date: 2026-07-29) |
| Primary citation | Caregnato, A.,Hohmann, U.,Hothorn, M. Structure of the Arabidopsis receptor kinase SRF6 ectodomain determined from crystals obtained using the LRR crystallization screen. Acta Crystallogr D Struct Biol, 82:800-812, 2026 Cited by PubMed Abstract: Plant-specific membrane receptor kinases with structurally diverse extracellular domains regulate key processes in plant growth, development, immunity and symbiosis. Structural studies of these glycoproteins are often hampered by the limited quantities in which they can be obtained. Here, we describe the leucine-rich repeat (LRR) crystallization screen, which has enabled the successful crystallization and structure determination of multiple receptor kinase ectodomains, including ligand- and co-receptor-bound complexes. As an example, we report the 1.5 Å resolution crystal structure of the LRR domain of STRUBBELIG-RECEPTOR FAMILY 6 (SRF6) from Arabidopsis thaliana. The SRF6 ectodomain contains seven LRRs and a disulfide-bond-stabilized N-terminal capping domain but lacks the canonical C-terminal cap and the N-glycosylation pattern typically found in other family members. Previously reported protein-protein interactions between the SRF6 and SRF7 ectodomains and the receptor kinases BRI1, BRL1, BRL3, SERK3 and BIR1-BIR3 could not be confirmed by quantitative isothermal titration calorimetry and grating-coupled interferometry assays, suggesting that these structurally conserved LRR receptor kinases may have signalling functions outside the brassinosteroid pathway. PubMed: 42283205DOI: 10.1107/S2059798326005498 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.501 Å) |
Structure validation
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