期刊
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY
卷 74, 期 -, 页码 671-680出版社
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S205979831800774X
关键词
malectin-like receptor kinases; plant reproductive signalling; cell-wall signalling; membrane signalling; Arabidopsis; cell signalling; membrane receptors; receptor kinases; Catharanthus roseus
资金
- European Research Council (ERC) under the European Union's Horizon 2020 Research and Innovation Programme [716358]
- Swiss National Science Foundation Ambizione Program [P200P3_161534]
- SNF [31003A_173101]
- Fondation de Famille Sandoz
- EMBO long-term fellowship [ALTF 1004-2017]
- Swiss National Science Foundation (SNF) [31003A_173101] Funding Source: Swiss National Science Foundation (SNF)
- European Research Council (ERC) [716358] Funding Source: European Research Council (ERC)
Complex cell-to-cell communication between the male pollen tube and the female reproductive organs is required for plant fertilization. A family of Catharanthus roseus receptor kinase 1-like (CrRLK1L) membrane receptors has been genetically implicated in this process. Here, crystal structures of the CrRLK1Ls ANXUR1 and ANXUR2 are reported at 1.48 and 1.1 angstrom resolution, respectively. The structures reveal a novel arrangement of two malectin-like domains connected by a short -hairpin linker and stabilized by calcium ions. The canonical carbohydrate-interaction surfaces of related animal and bacterial carbohydrate-binding modules are not conserved in plant CrRLK1Ls. In line with this, the binding of chemically diverse oligosaccharides to ANXUR1 and HERCULES1 could not be detected. Instead, CrRLK1Ls have evolved a protein-protein interface between their malectin domains which forms a deep cleft lined by highly conserved aromatic and polar residues. Analysis of the glycosylation patterns of different CrRLK1Ls and their oligomeric states suggests that this cleft could resemble a binding site for a ligand required for receptor activation of CrRLK1Ls.
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